The DOI matches its Crossref record; 58 of the 59 references it cites were found in a registry or an index.
Solution Structure of the KIX Domain of CBP Bound to the Transactivation Domain of CREB: A Model for Activator:Coactivator Interactions
Open accessAbstract
The nuclear factor CREB activates transcription of target genes in part through direct interactions with the KIX domain of the coactivator CBP in a phosphorylation-dependent manner. The solution structure of the complex formed by the phosphorylated kinase-inducible domain (pKID) of CREB with KIX reveals that pKID undergoes a coil-->helix folding transition upon binding to KIX, forming two alpha helices. The amphipathic helix alphaB of pKID interacts with a hydrophobic groove defined by helices alpha1 and alpha3 of KIX. The other pKID helix, alphaA, contacts a different face of the alpha3 helix. The phosphate group of the critical phosphoserine residue of pKID forms a hydrogen bond to the side chain of Tyr-658 of KIX. The structure provides a model for interactions between other transactivation domains and their targets.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“a single hydrogen bond between this phosphoserine and a tyrosine residue within CBP is critical for complexation”
From Assembly requirements of PU.1–Pip (IRF‐4) activator complexes: inhibiting function in vivo using fused dimers (1999) · cites this paper as Radhakrishnan et al., 1997
Citations
Cites
Basic local alignment search tool
Altschul, S. F., Gish, W., Miller, W., Myers, E. W., & Lipman, D. J. (1990) · Journal of Molecular Biology · doi:10.1006/jmbi.1990.9999 · Cited by 98,669
AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR
Laskowski, R., Rullmann, J. A., MacArthur, M., Kaptein, R., & Thornton, J. (1996) · Journal of Biomolecular NMR · doi:10.1007/bf00228148 · Cited by 5,502
Nicholls, A. O., Sharp, K. A., & Honig, B. H. (1991) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.340110407 · Cited by 5,230
The Transcriptional Coactivators p300 and CBP Are Histone Acetyltransferases
Ogryzko, V. V., Schiltz, R. L., Russanova, V., Howard, B. H., & Nakatani, Y. (1996) · Cell · doi:10.1016/s0092-8674(00)82001-2 · Cited by 2,952
Cyclic AMP stimulates somatostatin gene transcription by phosphorylation of CREB at serine 133
Gonzalez, G. A., & Montminy, M. (1989) · Cell · doi:10.1016/0092-8674(89)90013-5 · Cited by 2,464
Self-citationStructure of the MDM2 Oncoprotein Bound to the p53 Tumor Suppressor Transactivation Domain
Kussie, P. H., Gorina, S., Marechal, V., Elenbaas, B., Moreau, J., Levine, A. J., & Pavletich, N. P. (1996) · Science · doi:10.1126/science.274.5289.948 · Cited by 2,206
Kamei, Y., Xu, L., Heinzel, T., Torchia, J., Kurokawa, R., Gloss, B., Lin, S.-C., Heyman, R. A., Rose, D. W., Glass, C. K., et al. (1996) · Cell · doi:10.1016/s0092-8674(00)81118-6 · Cited by 2,150
Phosphorylated CREB binds specifically to the nuclear protein CBP
Chrivia, J. C., Kwok, R. P. S., Lamb, N., Hagiwara, M., Montminy, M. R., & Goodman, R. H. (1993) · Nature · doi:10.1038/365855a0 · Cited by 2,052
Self-citationThe CBP co-activator is a histone acetyltransferase
Bannister, A. J., & Kouzarides, T. (1996) · Nature · doi:10.1038/384641a0 · Cited by 1,828
Knighton, D. R., Zheng, J., Eyck, L. F. T., Ashford, V. A., Xuong, N., Taylor, S. S., & Sowadski, J. M. (1991) · Science · doi:10.1126/science.1862342 · Cited by 1,764
Nuclear protein CBP is a coactivator for the transcription factor CREB
Kwok, R. P. S., Lundblad, J. R., Chrivia, J. C., Richards, J. P., Bächinger, H. P., Brennan, R. G., Roberts, S. G. E., Green, M. R., & Goodman, R. H. (1994) · Nature · doi:10.1038/370223a0 · Cited by 1,443
Transcriptional activation by recruitment
Ptashne, M., & Gann, A. (1997) · Nature · doi:10.1038/386569a0 · Cited by 1,158
Spera, S., & Bax, A. (1991) · Journal of the American Chemical Society · doi:10.1021/ja00014a071 · Cited by 1,101
PROMOTIF—A program to identify and analyze structural motifs in proteins
Hutchinson, E. G., & Thornton, J. M. (1996) · Protein Science · doi:10.1002/pro.5560050204 · Cited by 1,043
Knighton, D. R., Zheng, J., Eyck, L. F. T., Xuong, N., Taylor, S. S., & Sowadski, J. M. (1991) · Science · doi:10.1126/science.1862343 · Cited by 960
Role of CBP/P300 in nuclear receptor signalling
Chakravarti, D., LaMorte, V. J., Nelson, M. C., Nakajima, T., Schulman, I. G., Juguilon, H., Montminy, M., & Evans, R. M. (1996) · Nature · doi:10.1038/383099a0 · Cited by 932
Self-citationGonzalez, G. A., Yamamoto, K. K., Fischer, W. H., Karr, D., Menzel, P., Biggs, W., Vale, W., & Montminy, M. (1989) · Nature · doi:10.1038/337749a0 · Cited by 875
Self-citationThe application visualization system: a computational environment for scientific visualization
Upson, C. D., Faulhaber, T. A., Kamins, D., Laidlaw, D. H., Schlegel, D. R., Vroom, J., Gurwitz, R. F., & van Dam, A. (1989) · IEEE Computer Graphics and Applications · doi:10.1109/38.31462 · Cited by 830
Güntert, P., Braun, W. A., & Kurt Wüthrich, A. (1991) · Journal of Molecular Biology · doi:10.1016/0022-2836(91)90754-t · Cited by 784
Methodological advances in protein NMR
Bax, A., & Grzesiek, S. (1993) · Accounts of Chemical Research · doi:10.1021/ar00028a001 · Cited by 775
Amino‐aromatic interactions in proteins
Burley, S. K., & Petsko, G. A. (1986) · FEBS Letters · doi:10.1016/0014-5793(86)80730-x · Cited by 769
Activation of cAMP and mitogen responsive genes relies on a common nuclear factor
Arias, J., Alberts, A. S., Brindle, P. K., Claret, F. X., Smeal, T., Karin, M., Feramisco, J. R., & Montminy, M. (1994) · Nature · doi:10.1038/370226a0 · Cited by 726
Self-citationMethodological Advances in Protein NMR
Bax, A., & Grzesiek, S. (1993) · doi:10.1007/978-1-349-12749-8_2 · Cited by 716
Waksman, G., Kominos, D., Robertson, S. C., Pant, N., Baltimore, D., Birge, R. B., Cowburn, D., Hanafusa, H., Mayer, B. J., Overduin, M., et al. (1992) · Nature · doi:10.1038/358646a0 · Cited by 675
RNA Helicase A Mediates Association of CBP with RNA Polymerase II
Nakajima, T., Uchida, C., Anderson, S. F., Lee, C.-G., Hurwitz, J., Parvin, J. D., & Montminy, M. (1997) · Cell · doi:10.1016/s0092-8674(00)80376-1 · Cited by 540
Self-citationCooperation of Stat2 and p300/CBP in signalling induced by interferon-α
Bhattacharya, S., Eckner, R., Grossman, S., Oldread, E., Arany, Z., D'Andrea, A., & Livingston, D. M. (1996) · Nature · doi:10.1038/383344a0 · Cited by 493
Hagiwara, M., Alberts, A. S., Brindle, P. K., Meinkoth, J. L., Feramisco, J. R., Deng, T., Karin, M., Shenolikar, S., & Montminy, M. (1992) · Cell · doi:10.1016/0092-8674(92)90537-m · Cited by 457
Self-citationYamazaki, T., Forman-Kay, J. D., & Kay, L. E. (1993) · Journal of the American Chemical Society · doi:10.1021/ja00076a099 · Cited by 444
Parker, D., Ferreri, K., Nakajima, T., Lamorte, V. J., Evans, R., Koerber, S. C., Hoeger, C., & Montminy, M. R. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.2.694 · Cited by 408
Self-citationStructure and ligand recognition of the phosphotyrosine binding domain of Shc
Zhou, M., Ravichandran, K. S., Olejniczak, E. T., Petros, A. M., Meadows, R. P., Sattler, M., Harlan, J. E., Wade, W. S., Burakoff, S. J., & Fesik, S. W. (1995) · Nature · doi:10.1038/378584a0 · Cited by 364
Kwok, R. P. S., Laurance, M. E., Lundblad, J. R., Goldman, P. S., Shih, H., Connor, L. M., Marriott, S. J., & Goodman, R. H. (1996) · Nature · doi:10.1038/380642a0 · Cited by 359
Brinkmann, U., Mattes, R., & Buckel, P. (1989) · Gene · doi:10.1016/0378-1119(89)90470-8 · Cited by 358
Otting, G., & Wüthrich, K. (1990) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583500005412 · Cited by 354
Kuboniwa, H., Grzesiek, S., Delaglio, F., & Bax, A. (1994) · Journal of Biomolecular NMR · doi:10.1007/bf00398416 · Cited by 344
CBP as a transcriptional coactivator of c-Myb.Preprint
Dai, P., Akimaru, H., Tanaka, Y., Hou, D., Yasukawa, T., Kanei‐Ishii, C., Takahashi, T., & Ishii, S. (1996) · Genes & Development · doi:10.1101/gad.10.5.528 · Cited by 343
Güntert, P., & Wüthrich, K. (1991) · Journal of Biomolecular NMR · doi:10.1007/bf02192866 · Cited by 331
The FSSP database of structurally aligned protein fold families.
Holm, L., & Sander, C. (1994) · Europe PMC (PubMed Central) · Cited by 315
(1995) · PubMed · Cited by 312
Amino/Aromatic Interactions in Proteins: Is the Evidence Stacked Against Hydrogen Bonding?
Mitchell, J. B. O., Nandi, C. L., McDonald, I. K., Thornton, J. M., & Price, S. L. (1994) · Journal of Molecular Biology · doi:10.1006/jmbi.1994.1370 · Cited by 303
Planar Stacking Interactions of Arginine and Aromatic Side-Chains in Proteins
Flocco, M. M., & Mowbray, S. L. (1994) · Journal of Molecular Biology · doi:10.1006/jmbi.1994.1022 · Cited by 293
Mayer, B. J., Jackson, P. K., Etten, R. A. V., & Baltimore, D. (1992) · Molecular and Cellular Biology · doi:10.1128/mcb.12.2.609 · Cited by 288
Induced α Helix in the VP16 Activation Domain upon Binding to a Human TAF
Uesugi, M., Nyanguile, O., Lu, H., Levine, A. J., & Verdine, G. L. (1997) · Science · doi:10.1126/science.277.5330.1310 · Cited by 284
Drosophila CBP is a co-activator of cubitus interruptus in hedgehog signalling
Akimaru, H., Chen, Y., Dai, P., Hou, D., Nonaka, M., Smolik, S. M., Armstrong, S., Goodman, R. H., & Ishii, S. (1997) · Nature · doi:10.1038/386735a0 · Cited by 282
[11] Multidimensional heteronuclear nuclear magnetic resonance of proteins
Clore, G. M., & Gronenborn, A. M. (1994) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(94)39013-4 · Cited by 273
Nakajima, T., Uchida, C., Anderson, S. F., Parvin, J. D., & Montminy, M. (1997) · Genes & Development · doi:10.1101/gad.11.6.738 · Cited by 238
Self-citationGonzalez, G. A., Menzel, P., Leonard, J., Fischer, W. H., & Montminy, M. (1991) · Molecular and Cellular Biology · doi:10.1128/mcb.11.3.1306 · Cited by 232
Self-citationTranscriptional control: Versatile molecular glue
Janknecht, R., & Hunter, T. R. (1996) · Current Biology · doi:10.1016/s0960-9822(02)00636-x · Cited by 231
Adaptor-mediated Recruitment of RNA Polymerase II to a Signal-dependent Activator
Kee, B. L., Arias, J., & Montminy, M. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.5.2373 · Cited by 205
Self-citationTriple post‐transcriptional control
Bechhofer, D. H. (1990) · Molecular Microbiology · doi:10.1111/j.1365-2958.1990.tb02051.x · Cited by 204
The cAMP-regulated transcription factor CREB interactswith a component of the TFIID complex.
Ferreri, K., Gill, G., & Montminy, M. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.4.1210 · Cited by 193
Self-citationBrindle, P. K., Linke, S., & Montminy, M. (1993) · Nature · doi:10.1038/364821a0 · Cited by 173
Self-citationLee, W., Revington, M., Arrowsmith, C. H., & Kay, L. E. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)00740-3 · Cited by 162
Vuister, G. W., Wang, A. C., & Bax, A. (1993) · Journal of the American Chemical Society · doi:10.1021/ja00065a071 · Cited by 144
A Structural Analysis of Phosphate and Sulphate Binding Sites in Proteins
Copley, R. R., & Barton, G. J. (1994) · Journal of Molecular Biology · doi:10.1006/jmbi.1994.1583 · Cited by 143
Regulation of the c-fos promoter by the ternary complex factor Sap-1a and its coactivator CBP.
Janknecht, R., & Nordheim, A. (1996) · PubMed · Cited by 120
Shih, H.-M., Goldman, P. S., DeMaggio, A. J., Hollenberg, S. M., Goodman, R. H., & Hoekstra, M. F. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.24.13896 · Cited by 100
Solid-state CD and peptide helical screw sense
Formaggio, F., Crisma, M., Toniolo, C., & Kamphuis, J. (1998) · Biopolymers · doi:10.1002/(sici)1097-0282(199603)38:3 · Cited by 27
Novel Pulse Sequences for the Resonance Assignment of Aromatic Side Chains in13C-Labeled Proteins
Löhr, F., & Rüterjans, H. (1996) · Journal of Magnetic Resonance Series B · doi:10.1006/jmrb.1996.0140 · Cited by 22
Research works printed but not linked: 1
- Bannister, 1995, Stimulation of c-Jun activity by CBP, Oncogene, 11, 2509
Cited by
Sorted by citations
Intrinsically unstructured proteins and their functions
Dyson, H. J., & Wright, P. E. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1589 · Cited by 3,871
Self-citationIntrinsically unstructured proteins: re-assessing the protein structure-function paradigm
Wright, P. E., & Dyson, H. J. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3110 · Cited by 2,968
Self-citationTranscriptional regulation by the phosphorylation-dependent factor CREB
Mayr, B., & Montminy, M. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35085068 · Cited by 2,587
Self-citationIntrinsically disordered proteins in cellular signalling and regulation
Wright, P. E., & Dyson, H. J. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3920 · Cited by 2,482
Self-citationCREB: A Stimulus-Induced Transcription Factor Activated by A Diverse Array of Extracellular Signals
Shaywitz, A. J., & Greenberg, M. E. (1999) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.68.1.821 · Cited by 2,133
Metadata
- Authors
- Radhakrishnan, I., Pérez-Alvarado, G. C., Parker, D., Dyson, H. J., Montminy, M. R., & Wright, P. E.
- Affiliations
- Scripps Research Institute (US)
- Joslin Diabetes Center (US)
- Corresponding author
- Wright, Peter E
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 1997-12
- Volume
- 91
- Issue
- 6
- Pages
- 741-752
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W1968910000
- Cited by
- 728
- References
- 59
- Citations by year
- 2026: 11 · 2025: 18 · 2024: 10 · 2023: 17 · 2022: 20 · 2021: 14 · 2020: 19 · 2019: 19 · 2018: 25 · 2017: 24 · 2016: 29 · 2015: 23 · 2014: 30 · 2013: 27 · 2012: 32
- FWCI
- 10.19
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (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 › Signaling Pathways in Disease
- Keywords
- CREB, CBP, KIX domain, transactivation domain, transcriptional coactivator, protein-protein interaction, amphipathic helix, hydrophobic groove, transcriptional activation, solution structure
- MeSH terms
- Amino Acid Sequence, Animals, Binding Sites, Humans, Models, Molecular, Molecular Sequence Data, Nuclear Proteins, Phosphopeptides, Protein Conformation, Transcription Factors, Trans-Activators, Consensus Sequence, Sequence Alignment, Cyclic AMP Response Element-Binding Protein, Sequence Homology, Amino Acid, Protein Structure, Secondary, Nuclear Magnetic Resonance, Biomolecular, CREB-Binding Protein
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
