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A new pattern for helix–turn–helix recognition revealed by the PU.l ETS–domain–DNA complex
Abstract
The Ets family of transcription factors, of which there are now about 35 members regulate gene expression during growth and development. They share a conserved domain of around 85 amino acids which binds as a monomer to the DNA sequence 5'-C/AGGAA/T-3'. We have determined the crystal structure of an ETS domain complexed with DNA, at 2.3-A resolution. The domain is similar to alpha + beta (winged) 'helix-turn-helix' proteins and interacts with a ten-base-pair region of duplex DNA which takes up a uniform curve of 8 degrees. The domain contacts the DNA by a novel loop-helix-loop architecture. Four of amino acids that directly interact with the DNA are highly conserved: two arginines from the recognition helix lying in the major groove, one lysine from the 'wing' that binds upstream of the core GGAA sequence, and another lysine, from the 'turn' of the 'helix-turn-helix' motif, which binds downstream and on the opposite strand.
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In the citing paper
“The crystal structure of the PU.1 DBD bound to DNA shows that the N-terminus of PU.1 faces the binding site for Pip (Kodandapani et al., 1996).”
From Assembly requirements of PU.1–Pip (IRF‐4) activator complexes: inhibiting function in vivo using fused dimers (1999) · cites this paper as Kodandapani et al., 1996
In the citing paper
“in the PU.1 DBD-DNA co-crystal structure, the N-terminus of PU.1 is adjacent to the predicted binding site of Pip.”
From Assembly requirements of PU.1–Pip (IRF‐4) activator complexes: inhibiting function in vivo using fused dimers (1999) · cites this paper as Kodandapani et al., 1996
In the citing paper
“This last suggestion is supported by the numerous protein-DNA backbone contacts observed in the PU.1-DNA co-crystal structure”
From Assembly requirements of PU.1–Pip (IRF‐4) activator complexes: inhibiting function in vivo using fused dimers (1999) · cites this paper as Kodandapani et al., 1996
In the citing paper
“In the crystal structure of PU.1-ETS domain-DNA complex, Kodandpani et al. showed that the ETS domain assumes a tight globular structure formed by three α-helices and a four-stranded anti-parallel β-sheet.”
From PU.1 and partners: regulation of haematopoietic stem cell fate in normal and malignant haematopoiesis (2009) · cites this paper as [47]
In the citing paper
“It binds to the 5′-GGAA-3′ core sequence in the major groove via the α3-recognition helix, whereas the two loops on both sides contact the phosphate backbone in the minor groove.”
From PU.1 and partners: regulation of haematopoietic stem cell fate in normal and malignant haematopoiesis (2009) · cites this paper as [47]
In the citing paper
“It has been shown in the crystal structure of PU.1 that its β3/β4 region does not interact with DNA, but is exposed to the solvent [47].”
From PU.1 and partners: regulation of haematopoietic stem cell fate in normal and malignant haematopoiesis (2009) · cites this paper as [47]
In the citing paper
“The C terminus of the PU.1 Ets-homology domain is a winged helix–turn–helix motif (8) that serves as a DNA binding domain.”
From Negative cross-talk between hematopoietic regulators: GATA proteins repress PU.1 (1999) · cites this paper as [8]
In the citing paper
“The overall structure and DNA-binding mechanism of the ETS domain is based on high-resolution molecular models of ten family members derived from both X-ray crystallography and nuclear magnetic resonance (NMR) spectroscopy (Figure 1b, Supplemental Table 2) (37–51).”
From Genomic and biochemical insights into the specificity of ETS transcription factors (2011) · cites this paper as [38]
Citations
Cites
Site-directed mutagenesis by overlap extension using the polymerase chain reaction
Ho, S. N., Hunt, H. D., Horton, R. M., Pullen, J. K., & Pease, L. R. (1989) · Gene · doi:10.1016/0378-1119(89)90358-2 · Cited by 7,354
Free R value: a novel statistical quantity for assessing the accuracy of crystal structures
Brünger, A. T. (1992) · Nature · doi:10.1038/355472a0 · Cited by 3,877
Conformation of Polypeptides and Proteins
Ramachandran, G. N., & Sasisekharan, V. (1968) · Advances in protein chemistry · doi:10.1016/s0065-3233(08)60402-7 · Cited by 2,950
Accurate Bond and Angle Parameters for X-ray Protein Structure Refinement
Engh, R., & Huber, R. (1991) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767391001071 · Cited by 2,497
Co-crystal structure of the HNF-3/fork head DNA-recognition motif resembles histone H5
Clark, K., Halay, E. D., Lai, E., & Burley, S. K. (1993) · Nature · doi:10.1038/364412a0 · Cited by 1,275
Crystal Structure of a CAP-DNA Complex: the DNA Is Bent by 90°
Schultz, S. C., Shields, G. C., & Steitz, T. A. (1991) · Science · doi:10.1126/science.1653449 · Cited by 1,116
Resolution of phase ambiguity in macromolecular crystallography
Wang, B. (1985) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(85)15009-3 · Cited by 1,033
The macrophage and B cell-specific transcription factor PU.1 is related to the ets oncogene
Klemsz, M. J., McKercher, S. R., Celada, A., Van Beveren, C., & Maki, R. A. (1990) · Cell · doi:10.1016/0092-8674(90)90219-5 · Cited by 954
Self-citationThe Ets family of transcription factors
Wasylyk, B., Hahn, S. L., & Giovane, A. (1993) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1993.tb19864.x · Cited by 839
Interactive computer graphics: FRODO
Jones, T. A. (1985) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(85)15014-7 · Cited by 825
Research works printed but not linked: 7
- Moreau-Gachelin, F. Biochim. biophys. Acta 1198, 149–163 (1994).
- Moreau-Gachelin, F., Mattei, M. G., Tambourin, R. & Tavitian, A. Oncogene 4, 1449–1456 (1989).
- Mavrothalassitis, G., Fisher, R. J., Smyth, F., Watson, D. K. & Papas, T. S. Oncogens 9, 425–435 (1994).
- Furey, W. & Swaminathan, S. Am. crystallogr. Ass. Meeting 18, 73 (1990).
- Jones, T. A., Zhou, J., Cowan, S. W. & Kjeldgaard, M. Acta crystallogr. A47, 110–119 (1992).
- Brünger, A. T. X-PLOR Manual Version 3.1 (Yale Univ. Press, New Haven, CT, 1992).
- Parkinson, G., Vojtechovsky, J., Clowney, L., Brünger, A. T. & Berman, H. M. Acta crystallogr. D52, 57–64 (1996).
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Rohs, R., Jin, X., West, S. M., Joshi, R., Honig, B. H., & Mann, R. S. (2010) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060408-091030 · Cited by 902
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Tenen, D. G., Hromas, R., Licht, J. D., & Zhang, D.-E. (1997) · Blood · doi:10.1182/blood.v90.2.489 · Cited by 735
Chinenov, Y. V., & Kerppola, T. K. (2001) · Oncogene · doi:10.1038/sj.onc.1204385 · Cited by 723
“This domain folds into a compact helix ± turn ± helix like structure with a single helix that forms base speci®c contacts in the major groove of DNA (Kodandapani et al., 1996) (Figure 3).”
BackgroundThe many faces of the helix-turn-helix domain: Transcription regulation and beyond
Aravind, L., Anantharaman, V., BALAJI, S., Babu, M. M., & IYER, L. (2005) · FEMS Microbiology Reviews · doi:10.1016/j.femsre.2004.12.008 · Cited by 734
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Dittmer, J. (2003) · Molecular Cancer · doi:10.1186/1476-4598-2-29 · Cited by 498
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Zhang, P., Behre, G., Pan, J., Iwama, A., Wara-aswapati, N., Radomska, H. S., Auron, P. E., Tenen, D. G., & Sun, Z. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.15.8705 · Cited by 459
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Xu, H. E., Rould, M. A., Xu, W., Epstein, J. A., Maas, R. L., & Pabo, C. O. (1999) · Genes & Development · doi:10.1101/gad.13.10.1263 · Cited by 311
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Batchelor, A. H., Piper, D. E., de la Brousse, F. C., McKnight, S. L., & Wolberger, C. (1998) · Science · doi:10.1126/science.279.5353.1037 · Cited by 291
Defective trophoblast function in mice with a targeted mutation of Ets2Preprint
Yamamoto, H., Flannery, M. L., Kupriyanov, S., Pearce, J., McKercher, S. R., Henkel, G. W., Maki, R. A., Werb, Z., & Oshima, R. G. (1998) · Genes & Development · doi:10.1101/gad.12.9.1315 · Cited by 292
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BackgroundSelf-citationStructural basis of DNA recognition by the heterodimeric cell cycle transcription factor E2F-DPPreprint
Zheng, N., Fraenkel, E., Pabo, C. O., & Pavletich, N. P. (1999) · Genes & Development · doi:10.1101/gad.13.6.666 · Cited by 271
“The winged-helix motif occurs in several eukaryotic transcription factors (for review, see Kaufmann and Knochel 1996), including HNF-3g (Clark et al. 1993), ETS1 (Kodandapani et al. 1996), and HSF (Harrison et al. 1994), as well as in the histone H5 globular domain (Ramakrishnan et al. 1993) (Fig.”
BackgroundMartı́nez-Hackert, E., & Stock, A. (1997) · Journal of Molecular Biology · doi:10.1006/jmbi.1997.1065 · Cited by 267
Luscombe, N., & Thornton, J. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00571-5 · Cited by 272
Vangala, R. K., Heiss-Neumann, M. S., Rangatia, J. S., Singh, S. M., Schoch, C., Tenen, D. G., Hiddemann, W., & Behre, G. (2003) · Blood · doi:10.1182/blood-2002-04-1288 · Cited by 245
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Mueller, B. U., Pabst, T., Osato, M., Asou, N., Johansen, L. M., Minden, M. D., Behre, G., Hiddemann, W., Ito, Y., & Tenen, D. G. (2002) · Blood · doi:10.1182/blood.v100.3.998 · Cited by 243
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BackgroundFujii, Y., Shimizu, T., Kusumoto, M., Kyogoku, Y., Taniguchi, T., & Hakoshima, T. (1999) · The EMBO Journal · doi:10.1093/emboj/18.18.5028 · Cited by 223
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Dickinson, L. A., Gulizia, R. J., Trauger, J. W., Baird, E. E., Mosier, D. E., Gottesfeld, J. M., & Dervan, P. B. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.22.12890 · Cited by 219
Jousset, C., Carron, C., Boureux, A., Quang, C. T., Oury, C., Dusanter‐Fourt, I., Charon, M., Levin, J., Bernard, O., & Ghysdael, J. (1997) · The EMBO Journal · doi:10.1093/emboj/16.1.69 · Cited by 207
Oettgen, P., Alani, R. M., Barcinski, M. A., Brown, L. F., Akbarali, Y., Boltax, J., KUNSCH, C. A., Münger, K., & Libermann, T. A. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.8.4419 · Cited by 217
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Karantzoulis-Fegaras, F., Antoniou, H., Lai, S.-L. M., Kulkarni, G., D'Abreo, C., Wong, G. K. T., Miller, T. L., Chan, Y., Atkins, J., Wang, Y., et al. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.5.3076 · Cited by 211
Brass, A. L., Zhu, A. Q., & Singh, H. (1999) · The EMBO Journal · doi:10.1093/emboj/18.4.977 · Cited by 204
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Breeze, A. L. (2000) · Progress in Nuclear Magnetic Resonance Spectroscopy · doi:10.1016/s0079-6565(00)00020-0 · Cited by 202
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Anderson, M. K., Weiss, A. H., Hernandez-Hoyos, G., Dionne, C. J., & Rothenberg, E. V. (2002) · Immunity · doi:10.1016/s1074-7613(02)00277-7 · Cited by 182
Tootle, T. L., & Rebay, I. (2005) · BioEssays · doi:10.1002/bies.20198 · Cited by 184
Lavallée, V., Baccelli, I., Krošl, J., Wilhelm, B. T., Barabé, F., Gendron, P., Boucher, G., Lemieux, S., Marinier, A., Meloche, S., et al. (2015) · Nature Genetics · doi:10.1038/ng.3371 · Cited by 168
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Nelson, H. C. M., & Littlefield, O. (1999) · Nature Structural Biology · doi:10.1038/8269 · Cited by 170
Fisher, R. C., & Scott, E. W. (1998) · STEM CELLS · doi:10.1002/stem.160025 · Cited by 158
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Oshima, R. G., Baribault, H., & Caul�n, C. (1996) · Cancer and Metastasis Reviews · doi:10.1007/bf00054012 · Cited by 156
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BackgroundThe structural basis for the oriented assembly of a TBP/TFB/promoter complex
Littlefield, O., Korkhin, Y., & Sigler, P. B. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.24.13668 · Cited by 154
Reddy, V. A., Iwama, A., Iotzova, G., Schulz, M., Elsasser, A., Vangala, R. K., Tenen, D. G., Hiddemann, W., & Behre, G. (2002) · Blood · doi:10.1182/blood.v100.2.483 · Cited by 152
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Cook, W. D., McCaw, B. J., Herring, C., John, D. L., Foote, S. J., Nutt, S. L., & Adams, J. M. (2004) · Blood · doi:10.1182/blood-2004-06-2234 · Cited by 140
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GA binding protein regulates interleukin 7 receptor α-chain gene expression in T cells
Xue, H., Bollenbacher, J., Rovella, V., Tripuraneni, R., Du, Y., Liu, C., Williams, A., McCoy, J. P., & Leonard, W. J. (2004) · Nature Immunology · doi:10.1038/ni1117 · Cited by 140
Molecular phylogeny of the ETS gene family
Laudet, V., Hänni, C., Stéhelin, D., & Duterque-Coquillaud, M. (1999) · Oncogene · doi:10.1038/sj.onc.1202444 · Cited by 139
“…Stockton Press All rights reserved 0950 ± 9232/99 $12.00 http://www.stockton-press.co.uk/onc protein, the HNF3/fork head family or the HSF (Heat Shock Factors) which all harbor a classical helix ± turn ± helix structure (Donalson et al., 1994, 1996; Liang et al., 1994; Kodandapani et al., 1996).”
BackgroundInfluentialJayaraman, G., Srinivas, R., Duggan, C. R., Ferreira, E., Swaminathan, S., Somasundaram, K., Williams, J. T., Hauser, C. A., Kurkinen, M. T., Dhar, R., et al. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.24.17342 · Cited by 140
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Weirauch, M. T., & Hughes, T. R. (2011) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-90-481-9069-0_3 · Cited by 135
Kitano, K., Kim, S., & Hakoshima, T. (2010) · Structure · doi:10.1016/j.str.2009.12.011 · Cited by 128
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Ternary complex factors: prime nuclear targets for mitogen-activated protein kinases
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Quinn, J. M., Barraco, P., Eriksson, M., & Merchant, S. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.9.6080 · Cited by 121
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“D55, 1421±1427 et al., 1995), transcription factor (Kodandapani et al., 1996) and streptavidin (Chilkoti et al., 1995), the latter binding its substrate, biotin, with an af®nity which is among the highest displayed for non-covalent interactions between a ligand and a protein (Ka ' 1013 Mÿ1).”
BackgroundSunnerhagen, M., Nilges, M., Otting, G., & Carey, J. (1997) · Nature Structural Biology · doi:10.1038/nsb1097-819 · Cited by 118
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BackgroundInfluentialEukaryotic transcription factors
Tan, S., & Richmond, T. J. (1998) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(98)80008-0 · Cited by 104
Expression of a novel factor in human breast cancer cells with metastatic potential.
Ree, A. H., Tvermyr, M., Engebraaten, O., Rooman, M. J., Røsok, Ø., Hovig, E. J., Meza‐Zepeda, L. A., Bruland, Ø. S., & Fodstad, Ø. (1999) · PubMed · Cited by 104
Binding to four‐way junction DNA: a common property of architectural proteins?
Zlatanova, J. S., & Holde, K. V. (1998) · The FASEB Journal · doi:10.1096/fasebj.12.6.421 · Cited by 104
The RUNX1–PU.1 axis in the control of hematopoiesis
Imperato, M. R., Cauchy, P., Obier, N., & Bonifer, C. (2015) · International Journal of Hematology · doi:10.1007/s12185-015-1762-8 · Cited by 94
The Transcription Factor PU.1 is a Critical Regulator of Cellular Communication in the Immune System
Turkistany, S. A., & DeKoter, R. P. (2011) · Archivum Immunologiae et Therapiae Experimentalis · doi:10.1007/s00005-011-0147-9 · Cited by 96
Szymczyna, B. R., & Arrowsmith, C. H. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m004294200 · Cited by 99
The Structural and Dynamic Basis of Ets-1 DNA Binding Autoinhibition
Lee, G. M., Donaldson, L. W., Pufall, M. A., Kang, H.-S., Pot, I., Graves, B. J., & McIntosh, L. P. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m410722200 · Cited by 95
Marmorstein, R., Mo, Y., Vaessen, B., & Johnston, K. (2000) · Nature Structural Biology · doi:10.1038/74055 · Cited by 95
Buijs, A., Rompaey, L. V., Molijn, A. C., Davis, J. N., Vertegaal, A. C. O., Potter, M. D., Adams, C., van Baal, S., Zwarthoff, E. C., Roussel, M. F., et al. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.24.9281-9293.2000 · Cited by 95
Morimoto, A. M., Jordan, K. C., Tietze, K., Britton, J. S., O’Neill, E., & Ruohola‐Baker, H. (1996) · Development · doi:10.1242/dev.122.12.3745 · Cited by 94
PU.1: A crucial and versatile player in hematopoiesis and leukemia
Kastner, P., & Chan, S. (2008) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2007.01.026 · Cited by 101
Stütz, A. M., & Woisetschläger, M. (1999) · PubMed · Cited by 86
The emergence of protein complexes: quaternary structure, dynamics and allostery
Perica, T., Marsh, J. A., Sousa, F. L., Natan, E., Colwell, L. J., Ahnert, S. E., & Teichmann, S. A. (2012) · Biochemical Society Transactions · doi:10.1042/bst20120056 · Cited by 83
Meraro, D., Gleit-Kielmanowicz, M., Hauser, H., & Levi, B.-Z. (2002) · The Journal of Immunology · doi:10.4049/jimmunol.168.12.6224 · Cited by 105
Véliz, E. A., Easterwood, L. M., & Beal, P. A. (2003) · Journal of the American Chemical Society · doi:10.1021/ja029742d · Cited by 82
Pio, F., Kodandapani, R., Ni, C.-Z., Shepard, W., Klemsz, M., McKercher, S. R., Maki, R. A., & Ely, K. R. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.38.23329 · Cited by 81
Self-citationRoss, I. L., Xie, Y., Ostrowski, M. C., & Hume, D. A. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.12.6662 · Cited by 79
Hill, D. A., Pedulla, M. L., & Reeves, R. (1999) · Nucleic Acids Research · doi:10.1093/nar/27.10.2135 · Cited by 79
Gupta, P., Gurudutta, G. U., Saluja, D., & Tripathi, R. P. (2009) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2009.00757.x · Cited by 74
Determinants of DNA-Binding Specificity of ETS-Domain Transcription Factors
Shore, P., Whitmarsh, A. J., Bhaskaran, R., Davis, R. J., Waltho, J. P., & Sharrocks, A. D. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.7.3338 · Cited by 78
PU.1/Interferon Regulatory Factor Interactions; Mechanisms of Transcriptional Regulation
Marecki, S., & Fenton, M. J. (2000) · Cell Biochemistry and Biophysics · doi:10.1385/cbb:33:2:127 · Cited by 74
Stütz, A. M., & Woisetschläger, M. (1999) · The Journal of Immunology · doi:10.4049/jimmunol.163.8.4383 · Cited by 94
“1 may contribute to the formation of a transcriptional competent complex by DNA bending, a feature also known for NFkB factors (43, 44).”
BackgroundEts regulation of the erbB2 promoter
Scott, G. K., Chang, C.-H., Erny-Albrecht, K. M., Xu, F., Fredericks, W. J., Rauscher, F. J., Thor, A. D., & Benz, C. C. (2000) · Oncogene · doi:10.1038/sj.onc.1204041 · Cited by 76
“…degrees of DNA bending induced by the truncated Ets domains from PU.1 and ESX/Elf-3 are in reasonable accord with the crystallographic results (Kodandapani et al., 1996), the enhanced bending observed by both of the full-length PU.1 and ESX/Elf-3 proteins is surprising given their lack of…”
BackgroundResultConstrained chromatin accessibility in PU.1-mutated agammaglobulinemia patients
Le Coz, C., Nguyen, D. N., Su, C., Nolan, B. E., Albrecht, A. V., Xhani, S., Sun, D., Demaree, B., Pillarisetti, P., Khanna, C., et al. (2021) · Journal of Experimental Medicine · doi:10.1084/jem.20201750 · Cited by 69
“1 ETS crystal structure is a winged helix-turn-helix motif containing three α-helices and a four-stranded β-sheet (Fig. 1 B; Kodandapani et al., 1996).”
BackgroundStructural mechanisms of human RecQ helicases WRN and BLM
Kitano, K. (2014) · Frontiers in Genetics · doi:10.3389/fgene.2014.00366 · Cited by 75
“RQC IS AN UNCONVENTIONAL WINGED-HELIX DOMAIN Figure 4 shows a comparison of the DNA-binding modes of the WRN (A) and BLM (B) RQC domains with those of the conventional winged-helix domains of the transcription factors ETS (Kodandapani et al., 1996; C) and RFX1 (Gajiwala et al., 2000; D).”
MethodMyeloid-specific gene expression
Clarke, S., & Gordon, S. (1998) · Journal of Leukocyte Biology · doi:10.1002/jlb.63.2.153 · Cited by 72
Transcriptional regulation during myelopoiesis
Lenny, N. T., Westendorf, J. J., & Hiebert, S. W. (1997) · Molecular Biology Reports · doi:10.1023/a:1006859700409 · Cited by 73
Metadata
- Authors
- Kodandapani, R., Pio, F., Ni, C.-Z., Piccialli, G., Klemsz, M., McKercher, S., Maki, R. A., & Ely, K. R.
- Affiliations
- Sanford Burnham Prebys Medical Discovery Institute (US)
- University of Naples Federico II (IT)
- Indiana University School of Medicine (US)
- Venue
- Nature
- Published
- 1996-04
- Volume
- 380
- Issue
- 6573
- Pages
- 456-460
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W1985177466
- Cited by
- 315
- References
- 23
- Citations by year
- 2026: 5 · 2025: 9 · 2024: 2 · 2023: 4 · 2022: 10 · 2021: 6 · 2020: 2 · 2019: 3 · 2018: 6 · 2017: 8 · 2016: 10 · 2015: 7 · 2014: 6 · 2013: 7 · 2012: 7
- FWCI
- 12.37
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA and Nucleic Acid Chemistry
- Keywords
- ETS transcription factors, ETS domain, DNA-binding domain, helix-turn-helix motif, winged helix-turn-helix, DNA recognition sequence, protein-DNA complex, crystal structure, major groove, transcriptional regulation
- MeSH terms
- Amino Acid Sequence, Animals, DNA, DNA-Binding Proteins, Humans, Models, Molecular, Molecular Sequence Data, Nucleic Acid Conformation, Protein Binding, Protein Conformation, Retroviridae Proteins, Oncogenic, Sequence Homology, Amino Acid, Crystallography, X-Ray, Helix-Turn-Helix Motifs
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