The DOI matches its Crossref record; 53 of the 54 references it cites were found in a registry or an index.
Structure of Full-Length HIV-1 CA: A Model for the Mature Capsid Lattice
Open accessAbstract
The capsids of mature retroviruses perform the essential function of organizing the viral genome for efficient replication. These capsids are modeled as fullerene structures composed of closed hexameric arrays of the viral CA protein, but a high-resolution structure of the lattice has remained elusive. A three-dimensional map of two-dimensional crystals of the R18L mutant of HIV-1 CA was derived by electron cryocrystallography. The docking of high-resolution domain structures into the map yielded the first unambiguous model for full-length HIV-1 CA. Three important protein-protein assembly interfaces are required for capsid formation. Each CA hexamer is composed of an inner ring of six N-terminal domains and an outer ring of C-terminal domains that form dimeric linkers connecting neighboring hexamers. Interactions between the two domains of CA further stabilize the hexamer and provide a structural explanation for the mechanism of action of known HIV-1 assembly inhibitors.
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
“In HIV six CA-NTDs form a hexameric ring with a central 18 helix bundle formed by helices 1, 2, and 3, providing the main intrahexamer stability”
From Retrovirus maturation-an extraordinary structural transformation (2016) · cites this paper as [52]
Citations
Cites
Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy
Henderson, R. A., Baldwin, J. M., Ceska, T. A., Zemlin, F., Beckmann, E., & Downing, K. H. (1990) · Journal of Molecular Biology · doi:10.1016/s0022-2836(05)80271-2 · Cited by 2,982
Automated molecular microscopy: The new Leginon system
Suloway, C. J. M., Pulokas, J., Fellmann, D., Cheng, A., Guerra, F., Quispe, J. D., Stagg, S. M., Potter, C. S., & Carragher, B. O. (2005) · Journal of Structural Biology · doi:10.1016/j.jsb.2005.03.010 · Cited by 1,695
Self-citationCrowther, R. A., Henderson, R. A., & Smith, J. M. (1996) · Journal of Structural Biology · doi:10.1006/jsbi.1996.0003 · Cited by 716
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 HIV-1 CA NTD is shaped as an arrowhead, with seven a helices (numbered 1–7) and an amino-terminal b-hairpin (Berthet-Colominas et al., 1999; Gamble et al., 1996; Gitti et al., 1996), while the CTD is more globular, with a single-turn 3 10 -helix and four short a helices (numbered 8–11)…”
Henderson, R. A., Baldwin, J. M., Downing, K. H., Lepault, J., & Zemlin, F. (1986) · Ultramicroscopy · doi:10.1016/0304-3991(86)90203-2 · Cited by 677
Assembly and Analysis of Conical Models for the HIV-1 Core
Ganser, B. K., Li, S., Klishko, V. Y., Finch, J. T., & Sundquist, W. I. (1999) · Science · doi:10.1126/science.283.5398.80 · Cited by 671
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 11×
“…CA proteins have revealed an atomic resolution model for the hexamer formed by the NTD of N-tropic murine leukemia virus (Mortuza et al., 2004) and several possible models for the CTD dimer (Gamble et al., 1997; Ivanov et al., 2007; Jin et al., 1999; Ternois et al., 2005; Worthylake et al., 1999).”
InfluentialThe stoichiometry of Gag protein in HIV-1
Briggs, J. A. G., Simon, M. N., Gross, I., Kräusslich, H.-G., Fuller, S. D., Vogt, V. M., & Johnson, M. C. (2004) · Nature Structural & Molecular Biology · doi:10.1038/nsmb785 · Cited by 539
Situs: A Package for Docking Crystal Structures into Low-Resolution Maps from Electron Microscopy
Wriggers, W. R., Milligan, R. A., & McCammon, J. A. (1999) · Journal of Structural Biology · doi:10.1006/jsbi.1998.4080 · Cited by 521
Three-dimensional structure determination by electron microscopy of two-dimensional crystals
Amos, L., Henderson, R. A., & Unwin, P. N. T. (1982) · Progress in Biophysics and Molecular Biology · doi:10.1016/0079-6107(83)90017-2 · Cited by 509
Image reconstructions of helical assemblies of the HIV-1 CA protein
Li, S., Hill, C. P., Sundquist, W. I., & Finch, J. T. (2000) · Nature · doi:10.1038/35030177 · Cited by 500
Structural organization of authentic, mature HIV‐1 virions and cores
Briggs, J. A. G., Wilk, T., Welker, R., Kräusslich, H., & Fuller, S. D. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg143 · Cited by 496
Structure 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
Functional Surfaces of the Human Immunodeficiency Virus Type 1 Capsid Protein
von Schwedler, U. K., Stray, K. M., Garrus, J. E., & Sundquist, W. I. (2003) · Journal of Virology · doi:10.1128/jvi.77.9.5439-5450.2003 · Cited by 421
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
Multi-resolution contour-based fitting of macromolecular structures
Chacón, P., & Wriggers, W. R. (2002) · Journal of Molecular Biology · doi:10.1006/jmbi.2002.5438 · Cited by 336
Crystal structure of dimeric HIV-1 capsid protein
Momany, C., Kovari, L. C., Prongay, A., Keller, W., Gitti, R. K., Lee, B. M., Gorbalenya, A. E., Tong, L., McClure, J., Ehrlich, L. S., et al. (1996) · Nature Structural & Molecular Biology · doi:10.1038/nsb0996-763 · Cited by 313
Assembly Properties of the Human Immunodeficiency Virus Type 1 CA Protein
Ganser-Pornillos, B. K., von Schwedler, U. K., Stray, K. M., Aiken, C., & Sundquist, W. I. (2004) · Journal of Virology · doi:10.1128/jvi.78.5.2545-2552.2004 · Cited by 302
Self-citationA conformational switch controlling HIV‐1 morphogenesis
Gross, I., Hohenberg, H., Wilk, T., Wiegers, K. J., Grättinger, M., Müller, B., Fuller, S., & Kräusslich, H. (2000) · The EMBO Journal · doi:10.1093/emboj/19.1.103 · Cited by 241
Retroviral Virions and Genomes
Vogt, V. (1997) · Europe PMC (PubMed Central) · Cited by 236
Structures of the HIV-1 capsid protein dimerization domain at 2.6 Å resolution
Worthylake, D. K., Wang, H., Yoo, S., Sundquist, W. I., & Hill, C. P. (1999) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444998007689 · Cited by 235
A peptide inhibitor of HIV-1 assembly in vitro
Sticht, J., Humbert, M., Findlow, S. C., Bodem, J., Müller, B., Dietrich, U., Werner, J. M., & Kräusslich, H. (2005) · Nature Structural & Molecular Biology · doi:10.1038/nsmb964 · Cited by 224
Antiviral Inhibition of the HIV-1 Capsid Protein
Tang, C., Loeliger, E., Kinde, I., Kyere, S., Mayo, K., Barklis, E., Sun, Y., Huang, M., & Summers, M. F. (2003) · Journal of Molecular Biology · doi:10.1016/s0022-2836(03)00289-4 · 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
Biochemical and Structural Analysis of Isolated Mature Cores of Human Immunodeficiency Virus Type 1
Welker, R., Hohenberg, H., Tessmer, U., Huckhagel, C., & Kräusslich, H. (2000) · Journal of Virology · doi:10.1128/jvi.74.3.1168-1177.2000 · Cited by 207
Lanman, J., Lam, T. T., Barnes, S., Sakalian, M., Emmett, M. R., Marshall, A. G., & Prevelige, P. E. (2003) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)01245-7 · Cited by 206
Structure of the N-terminal 283-residue fragment of the immature HIV-1 Gag polyprotein
Tang, C., Ndassa, Y., & Summers, M. F. (2002) · Nature Structural Biology · doi:10.1038/nsb806 · Cited by 205
Berthet-Colominas, C., Monaco, S., Novelli, A., Sibaı̈, G., Mallet, F., & Cusack, S. (1999) · The EMBO Journal · doi:10.1093/emboj/18.5.1124 · Cited by 191
Yeager, M., Wilson-Kubalek, E. M., Weiner, S. G., Brown, P. O., & Rein, A. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.13.7299 · Cited by 189
Self-citationHigh-resolution structure of a retroviral capsid hexameric amino-terminal domain
Mortuza, G. B., Haire, L. F., Stevens, A., Smerdon, S. J., Stoye, J. P., & Taylor, I. A. (2004) · Nature · doi:10.1038/nature02915 · Cited by 185
The HIV-1 capsid protein C-terminal domain in complex with a virus assembly inhibitor
Ternois, F., Sticht, J., Duquerroy, S., Kräusslich, H., & Rey, F. A. (2005) · Nature Structural & Molecular Biology · doi:10.1038/nsmb967 · Cited by 176
Gross, I., Hohenberg, H., Huckhagel, C., & Kräusslich, H. (1998) · Journal of Virology · doi:10.1128/jvi.72.6.4798-4810.1998 · Cited by 173
Key interactions in HIV-1 maturation identified by hydrogen-deuterium exchange
Lanman, J., Lam, T. T., Emmett, M. R., Marshall, A. G., Sakalian, M., & Prevelige, P. E. (2004) · Nature Structural & Molecular Biology · doi:10.1038/nsmb790 · Cited by 164
Valpuesta, J., Carrascosa, J. L., & Henderson, R. A. (1994) · Journal of Molecular Biology · doi:10.1006/jmbi.1994.1445 · Cited by 162
Göttlinger, H. G. (2001) · AIDS · doi:10.1097/00002030-200100005-00003 · Cited by 124
Association of Nef with the Human Immunodeficiency Virus Type 1 Core
Kotov, A., Zhou, J., Flicker, P. F., & Aiken, C. (1999) · Journal of Virology · doi:10.1128/jvi.73.10.8824-8830.1999 · Cited by 123
Campos-Olivas, R., Newman, J. L., & Summers, M. F. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3475 · Cited by 119
Model for lentivirus capsid core assembly based on crystal dimers of EIAV p26
Jin, Z., Jin, L., Peterson, D. L., & Lawson, C. L. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.2443 · Cited by 113
Structure and self-association of the Rous sarcoma virus capsid protein
Kingston, R. L., Fitzon-Ostendorp, T., Eisenmesser, E. Z., Schatz, G. W., Vogt, V. M., Post, C. B., & Rossmann, M. G. (2000) · Structure · doi:10.1016/s0969-2126(00)00148-9 · Cited by 112
Solution Structure of the Capsid Protein from the Human T-cell Leukemia Virus Type-I
Khorasanizadeh, S., Campos‐Olivas, R., & Summers, M. F. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.2986 · Cited by 101
The role of subunit hinges and molecular “switches” in the control of viral capsid polymorphism
Tang, J., Johnson, J. M., Dryden, K. A., Young, M., Zlotnick, A., & Johnson, J. E. (2006) · Journal of Structural Biology · doi:10.1016/j.jsb.2005.10.013 · Cited by 101
Domain-swapped dimerization of the HIV-1 capsid C-terminal domain
Ivanov, D., Tsodikov, O. V., Kasanov, J., Ellenberger, T., Wagner, G., & Collins, T. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0609477104 · Cited by 100
Briggs, J. A. G., Johnson, M. C., Simon, M. N., Fuller, S. D., & Vogt, V. M. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.10.025 · Cited by 89
Isolation of Human Immunodeficiency Virus Type 1 Cores: Retention of Vpr in the Absence of p6 gag
Accola, M. A., Öhagen, Å., & Göttlinger, H. G. (2000) · Journal of Virology · doi:10.1128/jvi.74.13.6198-6202.2000 · Cited by 79
Retrovirus Capsid Protein Assembly Arrangements
Mayo, K., Huseby, D. L., McDermott, J., Arvidson, B., Finlay, L. A., & Barklis, E. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)01176-2 · Cited by 75
Structural analysis of the N-terminal domain of the human T-cell leukemia virus capsid protein
Cornilescu, C. C., Bouamr, F., Yao, X., Carter, C., & Tjandra, N. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.4395 · Cited by 64
Implications for Viral Capsid Assembly from Crystal Structures of HIV-1 Gag1-278 and CAN133-278,
Kelly, B. N., Howard, B. R., Wang, H., Robinson, H. H., Sundquist, W. I., & Hill, C. P. (2006) · Biochemistry · doi:10.1021/bi060927x · Cited by 61
Second-Site Suppressors of Rous Sarcoma Virus CA Mutations: Evidence for Interdomain Interactions
Bowzard, J. B., Wills, J. W., & Craven, R. C. (2001) · Journal of Virology · doi:10.1128/jvi.75.15.6850-6856.2001 · 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
Morphogenesis and Maturation of Retroviruses
Kräusslich, H. (1996) · Current Topics in Microbiology and Immunology · doi:10.1007/978-3-642-80145-7 · Cited by 54
Analysis of rous sarcoma virus capsid protein variants assembled on lipid monolayers
Mayo, K., Vana, M. L., McDermott, J., Huseby, D. L., Leis, J. P., & Barklis, E. (2002) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.5354 · Cited by 42
Analysis of Mason-Pfizer Monkey Virus Gag Particles by Scanning Transmission Electron Microscopy
Parker, S., Wall, J. S., & Hunter, E. (2001) · Journal of Virology · doi:10.1128/jvi.75.19.9543-9548.2001 · Cited by 27
Cheng, A., & Yeager, M. J. (2004) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767304010396 · Cited by 14
Self-citation
Cited by
Sorted by citations
HIV-1 assembly, budding, and maturation
Sundquist, W. I., & Krausslich, H.-G. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006924 · Cited by 814
Mature HIV-1 capsid structure by cryo-electron microscopy and all-atom molecular dynamics
Zhao, G., Perilla, J. R., Yufenyuy, E. L., Meng, X., Chen, B., Ning, J., Ahn, J., Gronenborn, A. M., Schulten, K., Aiken, C., et al. (2013) · Nature · doi:10.1038/nature12162 · Cited by 801
X-Ray Structures of the Hexameric Building Block of the HIV Capsid
Pornillos, O., Ganser-Pornillos, B. K., Kelly, B. N., Hua, Y., Whitby, F. G., Stout, C. D., Sundquist, W. I., Hill, C. P., & Yeager, M. (2009) · Cell · doi:10.1016/j.cell.2009.04.063 · Cited by 523
Self-citationThe structural biology of HIV assembly
Ganser‐Pornillos, B. K., Yeager, M. J., & Sundquist, W. I. (2008) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2008.02.001 · Cited by 500
Self-citationHIV-1 capsid: the multifaceted key player in HIV-1 infection
Campbell, E. M., & Hope, T. J. (2015) · Nature Reviews Microbiology · doi:10.1038/nrmicro3503 · Cited by 430
Metadata
- Authors
- Ganser-Pornillos, B. K., Cheng, A., & Yeager, M.
- Affiliations
- Scripps Research Institute (US)
- Corresponding author
- Yeager, Mark
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2007-10
- Volume
- 131
- Issue
- 1
- Pages
- 70-79
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2034606779
- Cited by
- 321
- References
- 54
- Citations by year
- 2026: 8 · 2025: 4 · 2024: 8 · 2023: 3 · 2022: 7 · 2021: 16 · 2020: 18 · 2019: 15 · 2018: 6 · 2017: 19 · 2016: 11 · 2015: 23 · 2014: 16 · 2013: 28 · 2012: 26
- FWCI
- 10.46
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 2116 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- National Institute of General Medical Sciences (R01GM066087)
- National Institute of Allergy and Infectious Diseases (T32AI07244, T32AI007244)
- National Center for Research Resources (P41 RR17573, P41RR017573)
- Topics
- Life Sciences › Immunology and Microbiology › Virology › HIV Research and Treatment
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Advanced Electron Microscopy Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Keywords
- HIV-1 capsid protein, capsid lattice, hexamer assembly, protein-protein interaction, N-terminal domain, C-terminal domain, viral capsid structure
- MeSH terms
- Capsid, Humans, Models, Molecular, HIV-1, Crystallography, X-Ray, Cryoelectron Microscopy, Protein Structure, Quaternary, Capsid Proteins
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
