Structure of Full-Length HIV-1 CA: A Model for the Mature Capsid Lattice
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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.
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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.
“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]
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- 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
- Physical Sciences › Materials Science › Materials Chemistry › 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
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