Cited by 237HIV Research and TreatmentEnzyme Structure and FunctionProtein Structure and Dynamics

Structures of the HIV-1 capsid protein dimerization domain at 2.6 Å resolution

Worthylake, David K., Wang, Hui, Yoo, Sanghee, Sundquist, Wesley I., Hill, Christopher P.·1999·Acta Crystallographica Section D Biological Crystallography

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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Crossref · 10.1107/s0907444998007689

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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 and residues on helix 10 at the local three-fold.

    “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”

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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
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
  • Physical Sciences › Materials Science › Materials Chemistry › 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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