The DOI matches its Crossref record; 47 of the 47 references it cites were found in a registry or an index.
Structures of the HIV-1 capsid protein dimerization domain at 2.6 Å resolution
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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“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”
From Retrovirus maturation-an extraordinary structural transformation (2016) · cites this paper as [53]
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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-citationImage 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
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
Insights into RNA structure and function from genome-wide studies
Mortimer, S., Kidwell, M. A., & Doudna, J. A. (2014) · Nature Reviews Genetics · doi:10.1038/nrg3681 · Cited by 482
Metadata
- 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
- Licence
- 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
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › 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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