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Structures of the HIV-1 capsid protein dimerization domain at 2.6 Å resolution
Abstract
The human immunodeficiency virus type I (HIV-1) capsid protein is initially synthesized as the central domain of the Gag polyprotein, and is subsequently proteolytically processed into a discrete 231-amino-acid protein that forms the distinctive conical core of the mature virus. The crystal structures of two proteins that span the C-terminal domain of the capsid are reported here: one encompassing residues 146-231 (CA146-231) and the other extending to include the 14-residue p2 domain of Gag (CA146-p2). The isomorphous CA146-231 and CA146-p2 structures were determined by molecular replacement and have been refined at 2.6 A resolution to R factors of 22.3 and 20.7% (Rfree = 28.1 and 27.5%), respectively. The ordered domains comprise residues 148-219 for CA146-231 and 148-218 for CA146-p2, and their refined structures are essentially identical. The proteins are composed of a 310 helix followed by an extended strand and four alpha-helices. A crystallographic twofold generates a dimer that is stabilized by parallel packing of an alpha-helix 2 across the dimer interface and by packing of the 310 helix into a groove created by alpha-helices 2 and 3 of the partner molecule. CA146-231 and CA146-p2 dimerize with the full affinity of the intact capsid protein, and their structures therefore reveal the essential dimer interface of the HIV-1 capsid.
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“The CA-CTDs are located beneath the hexameric ring and form dimeric inter-hexamer interactions involving mainly hydrophobic interactions between residues on helix 9 at the local twofold [6,53] and residues on helix 10 at the local three-fold”
From Retrovirus maturation-an extraordinary structural transformation (2016) · cites this paper as [53]
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Cites
[20] Processing of X-ray diffraction data collected in oscillation mode
Otwinowski, Z., & Minor, W. (1997) · Methods in Enzymology · doi:10.1016/s0076-6879(97)76066-x · Cited by 33,475
Ellman, G. L. (1959) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(59)90090-6 · Cited by 26,824
PROCHECK: a program to check the stereochemical quality of protein structures
Laskowski, R. A., MacArthur, M. W., Moss, D. S., & Thornton, J. M. (1993) · Journal of Applied Crystallography · doi:10.1107/s0021889892009944 · Cited by 24,581
Jones, T. A., Zou, J.-Y., Cowan, S. W., & Kjeldgaard, M. (1991) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767390010224 · Cited by 12,616
Schägger, H., & von Jagow, G. (1987) · Analytical Biochemistry · doi:10.1016/0003-2697(87)90587-2 · Cited by 11,420
Solvent content of protein crystals
Matthews, B. W. (1968) · Journal of Molecular Biology · doi:10.1016/0022-2836(68)90205-2 · Cited by 7,970
[6] Use of T7 RNA polymerase to direct expression of cloned genes
Studier, F. W., Rosenberg, A. H., Dunn, J. J., & Dubendorff, J. W. (1990) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(90)85008-c · Cited by 6,562
Calculation of protein extinction coefficients from amino acid sequence data.
Gill, S., & von Hippel, P. H. (1989) · Analytical Biochemistry · doi:10.1016/0003-2697(89)90602-7 · Cited by 5,382
AMoRe: an automated package for molecular replacement
Navaza, J. (1994) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767393007597 · Cited by 4,941
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
X-PLOR Version 3.1: A System for X-ray Crystallography and NMR
Brünger, A. T. (1992) · Medical Entomology and Zoology · Cited by 3,424
Adachi, A., Gendelman, H. E., Koenig, S., Folks, T. M., Willey, R. L., Rabson, A. B., & Martín, M. Á. (1986) · Journal of Virology · doi:10.1128/jvi.59.2.284-291.1986 · Cited by 2,805
Determination of Macromolecular Structures from Anomalous Diffraction of Synchrotron Radiation
Hendrickson, W. A. (1991) · Science · doi:10.1126/science.1925561 · Cited by 1,131
Human Retroviruses and Aids - 1999
KUIKEN, C. L., & Foley, B. T. (1999) · doi:10.2172/1186019 · Cited by 952
Specific incorporation of cyclophilin A into HIV-1 virions
Franke, E. K., Yuan, H. E. H., & Luban, J. (1994) · Nature · doi:10.1038/372359a0 · Cited by 745
Crystal Structure of Human Cyclophilin A Bound to the Amino-Terminal Domain of HIV-1 Capsid
Gamble, T. R., Vajdos, F. F., Yoo, S., Worthylake, D. K., Houseweart, M., Sundquist, W. I., & Hill, C. P. (1996) · Cell · doi:10.1016/s0092-8674(00)81823-1 · Cited by 706 · cited 2×
“The three-dimensional structure of the N-terminal domain of the HIV-1 capsid has also been determined in solution (Gitti et al., 1996) and in crystals as complexes with an Fab fragment (Momany et al., 1996) and cyclophilin A (Gamble et al., 1996).”
Self-citationFunctional association of cyclophilin A with HIV-1 virions
Thali, M., Bukovsky, A., Kondo, E., Rosenwlrth, B., Walsh, C. T., Sodroski, J., & Göttlinger, H. G. (1994) · Nature · doi:10.1038/372363a0 · Cited by 629
Structure of the carboxyl-terminal dimerization domain of the HIV-1 capsid protein
Gamble, T. R., Yoo, S., Vajdos, F. F., von Schwedler, U. K., Worthylake, D. K., Wang, H., McCutcheon, J. P., Sundquist, W. I., & Hill, C. P. (1997) · Science · doi:10.1126/science.278.5339.849 · Cited by 598 · cited 12×
“The initial CA146±231 crystals diffracted poorly, however, and only allowed determination of an unre®ned CA146±231 structure at 3.0 AÊ resolution (Gamble et al., 1997).”
InfluentialSelf-citationStructure of the Amino-Terminal Core Domain of the HIV-1 Capsid Protein
Gitti, R. K., Lee, B. M., Walker, J., Summers, M. F., Yoo, S., & Sundquist, W. I. (1996) · Science · doi:10.1126/science.273.5272.231 · Cited by 459
Self-citationPettit, S. C., Moody, M. D., Wehbie, R. S., Kaplan, A. H., Nantermet, P. V., Klein, C. A., & Swanstrom, R. (1994) · Journal of Virology · doi:10.1128/jvi.68.12.8017-8027.1994 · Cited by 355
Proteolytic refolding of the HIV‐1 capsid protein amino‐terminus facilitates viral core assembly
von Schwedler, U. K., Stemmler, T. L., Klishko, V. Y., Li, S., Albertine, K. H., Davis, D. R., & Sundquist, W. I. (1998) · The EMBO Journal · doi:10.1093/emboj/17.6.1555 · Cited by 337
Self-citationMervis, R. J., Ahmad, N., Lillehoj, E. P., Raum, M. G., Salazar, F. H., Chan, H. W., & Venkatesan, S. (1988) · Journal of Virology · doi:10.1128/jvi.62.11.3993-4002.1988 · Cited by 309
Molecular recognition in the HIV-1 capsid/cyclophilin A complex 1 1Edited by J. A. Wells
Yoo, S., Myszka, D. G., Yeh, C.-Y., McMurray, M., Hill, C. P., & Sundquist, W. I. (1997) · Journal of Molecular Biology · doi:10.1006/jmbi.1997.1051 · Cited by 259
Self-citationRole of the major homology region of human immunodeficiency virus type 1 in virion morphogenesis
Mammano, F., Ohagen, A., Höglund, S., & Göttlinger, H. G. (1994) · Journal of Virology · doi:10.1128/jvi.68.8.4927-4936.1994 · Cited by 254
Functional domains of the capsid protein of human immunodeficiency virus type 1
Dorfman, T., Bukovský, A., Öhagen, Å., Höglund, S., & Göttlinger, H. G. (1994) · Journal of Virology · doi:10.1128/jvi.68.12.8180-8187.1994 · Cited by 218
Assembly of recombinant human immunodeficiency virus type 1 capsid protein in vitro
Ehrlich, L. S., Agresta, B. E., & Carter, C. A. (1992) · Journal of Virology · doi:10.1128/jvi.66.8.4874-4883.1992 · Cited by 218
Assembly, processing, and infectivity of human immunodeficiency virus type 1 gag mutants
Wang, C. T., & Barklis, E. (1993) · Journal of Virology · doi:10.1128/jvi.67.7.4264-4273.1993 · Cited by 184
Reicin, A., Paik, S., Berkowitz, R., Luban, J., Lowy, I., & Goff, S. (1995) · Journal of Virology · doi:10.1128/jvi.69.2.642-650.1995 · Cited by 155
Genetic analysis of the major homology region of the Rous sarcoma virus Gag protein
Craven, R. C., Leure‐Dupree, A. E., Weldon, R. A., & Wills, J. W. (1995) · Journal of Virology · doi:10.1128/jvi.69.7.4213-4227.1995 · Cited by 152
Reicin, A. S., Öhagen, Å., Yin, L., Höglund, S., & Goff, S. P. (1996) · Journal of Virology · doi:10.1128/jvi.70.12.8645-8652.1996 · Cited by 125
Srinivasakumar, N., Hammarskjöld, M. L., & Rekosh, D. M. (1995) · Journal of Virology · doi:10.1128/jvi.69.10.6106-6114.1995 · Cited by 113
Jowett, J. B. M., HOCKLEY, D. J., Nermut, M. V., & Jones, I. M. (1992) · Journal of General Virology · doi:10.1099/0022-1317-73-12-3079 · Cited by 113
Specificity and sequence requirements for interactions between various retroviral Gag proteins
Franke, E. K., Yuan, H. E., Bossolt, K. L., Goff, S. P., & Luban, J. (1994) · Journal of Virology · doi:10.1128/jvi.68.8.5300-5305.1994 · Cited by 109
Ramakrishnan, V., & Biou, V. (1997) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(97)76077-4 · Cited by 101
Identification of a Region in the Pr55gag-Polyprotein Essential for HIV-1 Particle Formation
von Poblotzki, A., Wagner, R., Niedrig, M., Wanner, G., Wolf, H. J., & Modrow, S. (1993) · Virology · doi:10.1006/viro.1993.1210 · Cited by 85
Chazal, N., Carrière, C., Gay, B., & Boulanger, P. A. (1994) · Journal of Virology · doi:10.1128/jvi.68.1.111-122.1994 · Cited by 81
McDermott, J., Farrell, L. E., Ross, R., & Barklis, E. (1996) · Journal of Virology · doi:10.1128/jvi.70.8.5106-5114.1996 · Cited by 62
Carrière, C., Gay, B., Chazal, N., Morin, N., & Boulanger, P. A. (1995) · Journal of Virology · doi:10.1128/jvi.69.4.2366-2377.1995 · Cited by 62
Hong, S. S., & Boulanger, P. A. (1993) · Journal of Virology · doi:10.1128/jvi.67.5.2787-2798.1993 · Cited by 59
Gowda, S. D., Stein, B. S., & Engleman, E. G. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)81809-9 · Cited by 58
Characterization of HIV‐1 p24 self‐association using analytical affinity chromatography
Rosé, S. D., Hensley, P., O'Shannessy, D. J., Culp, J. S., Debouck, C. M., & CHAIKEN, I. M. (1992) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.340130204 · Cited by 54
Mutations in the Ty3 major homology region affect multiple steps in Ty3 retrotransposition
Orlinsky, K. J., Gu, J., Hoyt, M., Sandmeyer, S. B., & Menees, T. M. (1996) · Journal of Virology · doi:10.1128/jvi.70.6.3440-3448.1996 · Cited by 50
Zhang, W., HOCKLEY, D. J., Nermut, M. V., Morikawa, Y., & Jones, I. M. (1996) · Journal of General Virology · doi:10.1099/0022-1317-77-4-743 · Cited by 47
A major retroviral core protein related to EPA and TIMP
Patarca, R., & Haseltine, W. A. (1985) · Nature · doi:10.1038/318390a0 · Cited by 41
Brooks, I. S., Watts, D. G., Soneson, K. K., & Hensley, P. (1994) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(94)40060-1 · Cited by 31
Spectral Analysis and Tryptic Susceptibility as Probes of HIV-1 Capsid Protein Structure
Ehrlich, L. S., Agresta, B. E., Gelfand, C. A., Jentoft, J. E., & Carter, C. A. (1994) · Virology · doi:10.1006/viro.1994.1565 · Cited by 24
Complementation of Human Immunodeficiency Virus (HIV-1) Gag Particle Formation
Zhao, Y., Jones, I. M., HOCKLEY, D. J., Nermut, M. V., & Roy, P. (1994) · Virology · doi:10.1006/viro.1994.1138 · Cited by 20
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Metadata
- Authors
- Worthylake, D. K., Wang, H., Yoo, S., Sundquist, W. I., & Hill, C. P.
- Affiliations
- University of Utah (US)
- Venue
- Acta Crystallographica Section D Biological Crystallography
- Published
- 1999-01-01
- Volume
- 55
- Issue
- 1
- Pages
- 85-92
- ISSN
- 0907-4449 (ISSN-L)
- OpenAlex
- W2159504933
- Cited by
- 235
- References
- 47
- Citations by year
- 2026: 4 · 2025: 1 · 2024: 1 · 2023: 1 · 2022: 3 · 2021: 4 · 2020: 2 · 2019: 6 · 2018: 5 · 2017: 13 · 2016: 13 · 2015: 9 · 2014: 7 · 2013: 13 · 2012: 18
- FWCI
- 1.96
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- Locations
- Acta Crystallographica Section D Biological Crystallography (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5r01ai043036-05, 5r01ai040333-04)
- National Institute of Allergy and Infectious Diseases (R01 AI40333, R01 AI43036)
- Topics
- Life Sciences › Immunology and Microbiology › Virology › HIV Research and Treatment
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- HIV-1 capsid protein, P2 domain, Gag protein, protein dimerization, dimer interface, 310-helix, alpha-helix packing, crystal structure, HIV-1
- MeSH terms
- Amino Acid Sequence, Capsid, Humans, Models, Molecular, Molecular Sequence Data, Peptide Fragments, Protein Conformation, Recombinant Proteins, HIV-1, Crystallography, X-Ray, Dimerization
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