The DOI matches its Crossref record; 29 of the 29 references it cites were found in a registry or an index.
High-resolution structure of a retroviral capsid hexameric amino-terminal domain
Abstract
Retroviruses are the aetiological agents of a range of human diseases including AIDS and T-cell leukaemias. They follow complex life cycles, which are still only partly understood at the molecular level. Maturation of newly formed retroviral particles is an essential step in production of infectious virions, and requires proteolytic cleavage of Gag polyproteins in the immature particle to form the matrix, capsid and nucleocapsid proteins present in the mature virion. Capsid proteins associate to form a dense viral core that may be spherical, cylindrical or conical depending on the genus of the virus. Nonetheless, these assemblies all appear to be composed of a lattice formed from hexagonal rings, each containing six capsid monomers. Here, we describe the X-ray structure of an individual hexagonal assembly from N-tropic murine leukaemia virus (N-MLV). The interface between capsid monomers is generally polar, consistent with weak interactions within the hexamer. Similar architectures are probably crucial for the regulation of capsid assembly and disassembly in all retroviruses. Together, these observations provide new insights into retroviral uncoating and how cellular restriction factors may interfere with viral replication.
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“While in-virus structures are currently lacking, these in vitro studies indicate that the arrangement of CA in mature retroviruses is well conserved”
From Retrovirus maturation-an extraordinary structural transformation (2016) · cites this paper as [11]
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Cites
Automated MAD and MIR structure solution
Terwilliger, T. C., & Berendzen, J. (1999) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444999000839 · Cited by 3,032
The cytoplasmic body component TRIM5α restricts HIV-1 infection in Old World monkeys
Stremlau, M. H., Owens, C. M., Perron, M. J., Kießling, M. K., Autissier, P., & Sodroski, J. (2004) · Nature · doi:10.1038/nature02343 · Cited by 1,810
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 1×
“However, structures of the mature forms of viral capsid protein NTDs have all been determined in monomeric or a non-biologically relevant dimeric for”
BackgroundThe 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
Synthesis, Assembly, and Processing of Viral Proteins
Swanstrom, R. I., & Wills, J. (1997) · Europe PMC (PubMed Central) · Cited by 518
Forshey, B. M., von Schwedler, U. K., Sundquist, W. I., & Aiken, C. (2002) · Journal of Virology · doi:10.1128/jvi.76.11.5667-5677.2002 · Cited by 514
ARP⧸wARP and Automatic Interpretation of Protein Electron Density Maps
Morris, R. J., Anastassis Perrakis, A., & Lamzin, V. S. (2003) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(03)74011-7 · Cited by 508
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
Positional cloning of the mouse retrovirus restriction gene Fvl
Best, S., Tissier, P. L., Towers, G. J., & Stoye, J. P. (1996) · Nature · doi:10.1038/382826a0 · Cited by 499
Self-citationStructural 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
Research works printed but not linked: 1
- Cowtan, K. ‘dm’: an automated procedure for phase improvement by density modification. Joint CCP4 ESF-EACBM Newsl. Prot. Crystallogr. 31, 34–38 (1994)
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Sundquist, W. I., & Krausslich, H.-G. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006924 · Cited by 814
TRIM family proteins: retroviral restriction and antiviral defence
Nisole, S., Stoye, J. P., & Saïb, A. (2005) · Nature Reviews Microbiology · doi:10.1038/nrmicro1248 · Cited by 761
Self-citationStremlau, M. H., Perron, M. J., Lee, M. N., Li, Y., Song, B., Javanbakht, H., Diaz‐Griffero, F., Anderson, D. J., Sundquist, W. I., & Sodroski, J. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0509996103 · Cited by 736
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
The 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
Metadata
- Authors
- Mortuza, G. B., Haire, L. F., Stevens, A., Smerdon, S. J., Stoye, J. P., & Taylor, I. A.
- Affiliations
- National Institute for Medical Research (GB)
- Corresponding author
- Taylor, Ian A.
- Venue
- Nature
- Published
- 2004-09-23
- Volume
- 431
- Issue
- 7007
- Pages
- 481-485
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2055643881
- Cited by
- 185
- References
- 29
- Citations by year
- 2025: 2 · 2023: 1 · 2022: 1 · 2021: 1 · 2020: 3 · 2019: 4 · 2018: 5 · 2017: 4 · 2016: 8 · 2015: 7 · 2014: 8 · 2013: 11 · 2012: 15
- FWCI
- 6.12
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Science and Technology Facilities Council (submittedVersion)
- Funders
- National Institutes of Health
- Topics
- Life Sciences › Immunology and Microbiology › Virology › HIV Research and Treatment
- Life Sciences › Immunology and Microbiology › Immunology › T-cell and Retrovirus Studies
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Keywords
- retroviral capsid, N-terminal domain, capsid assembly, capsid disassembly, viral uncoating, Gag protein, capsid lattice, cellular restriction factors, viral replication
- MeSH terms
- Amino Acid Sequence, Binding Sites, Capsid, Models, Molecular, Molecular Sequence Data, Leukemia Virus, Murine, Protein Structure, Tertiary, Crystallography, X-Ray, Virus Assembly, Protein Structure, Quaternary, Capsid Proteins
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