Cited by 327HIV Research and TreatmentAdvanced Electron Microscopy Techniques and ApplicationsEnzyme Structure and Function

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Structure of Full-Length HIV-1 CA: A Model for the Mature Capsid Lattice

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Ganser-Pornillos, Barbie K., Cheng, Anchi, Yeager, Mark·2007·Cell

DOI 10.1016/j.cell.2007.08.018

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Abstract

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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Authors: Ganser-Pornillos, B. K., Cheng, A., & Yeager, M.
Affiliations: Scripps Research Institute (US)
Corresponding author: Yeager, Mark
ORCID: Cheng, Anchi
Yeager, Mark
Venue: Cell
Publisher: Elsevier BV
Published: 2007-10
Volume: 131
Issue: 1
Pages: 70-79
ISSN: 0092-8674 (ISSN-L)
DOI: 10.1016/j.cell.2007.08.018
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

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Structure of Full-Length HIV-1 CA: A Model for the Mature Capsid Lattice

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