Structure of the Amino-Terminal Core Domain of the HIV-1 Capsid Protein
Abstract
The three-dimensional structure of the amino-terminal core domain (residues 1 through 151) of the human immunodeficiency virus-type 1 (HIV-1) capsid protein has been solved by multidimensional heteronuclear magnetic resonance spectroscopy. The structure is unlike those of previously characterized viral coat proteins and is composed of seven α helices, two β hairpins, and an exposed partially ordered loop. The domain is shaped like an arrowhead, with the β hairpins and loop exposed at the trailing edge and the carboxyl-terminal helix projecting from the tip. The proline residue Pro 1 forms a salt bridge with a conserved, buried aspartate residue (Asp 51 ), which suggests that the amino terminus of the protein rearranges upon proteolytic maturation. The binding site for cyclophilin A, a cellular rotamase that is packaged into the HIV-1 virion, is located on the exposed loop and encompasses the essential proline residue Pro 90 . In the free monomeric domain, Pro 90 adopts kinetically trapped cis and trans conformations, raising the possibility that cyclophilin A catalyzes interconversion of the cis- and trans- Pro 90 loop structures.
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A beta-hairpin is formed by the N-terminal residues in mature-like CA, stabilized by a salt bridge between the N-terminal proline and a conserved aspartate in helix 3.
“A beta-hairpin is formed by the N-terminal residues in mature-like CA, stabilized by a salt bridge between the N-terminal proline and a conserved aspartate in helix 3”
From Retrovirus maturation-an extraordinary structural transformation (2016) · cites this paper as [71]
In vivo, other viral components modulate mature core assembly, including integrase, the RNP, and the viral membrane.
“in vivo other viral components modulate mature core assembly, including integrase [75,76 ], the RNP [77], and the viral membrane [78].”
From Retrovirus maturation-an extraordinary structural transformation (2016) · cites this paper as [76]
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- Authors
- Gitti, R. K., Lee, B. M., Walker, J., Summers, M. F., Yoo, S., & Sundquist, W. I.
- Affiliations
- Howard Hughes Medical Institute (US)
- University of Utah (US)
- Corresponding author
- Gitti, Rossitza K.
- Lee, Brian M.
- Summers, Michael F.
- Sundquist, Wesley I.
- Venue
- Science
- Published
- 1996-07-12
- Volume
- 273
- Issue
- 5272
- Pages
- 231-235
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2015090760
- Cited by
- 459
- References
- 6
- Citations by year
- 2026: 6 · 2025: 2 · 2024: 5 · 2023: 7 · 2022: 7 · 2021: 10 · 2020: 3 · 2019: 6 · 2018: 5 · 2017: 10 · 2016: 11 · 2015: 15 · 2014: 15 · 2013: 21 · 2012: 15
- FWCI
- 7.08
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Cancer Institute (CA42014, P30CA042014)
- National Institute of General Medical Sciences (GM-42561)
- National Institute of Allergy and Infectious Diseases (AI30917)
- Topics
- Life Sciences › Immunology and Microbiology › Virology › HIV Research and Treatment
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Health Sciences › Medicine › Infectious Diseases › HIV/AIDS drug development and treatment
- Keywords
- HIV-1 capsid protein, protein structure, alpha-helix, beta-hairpin, salt bridges, proteolytic maturation, cyclophilin A, proline cis-trans isomerization, capsid protein, HIV-1 virions
- MeSH terms
- Amino Acid Isomerases, Amino Acid Sequence, Aspartic Acid, Binding Sites, Capsid, Carrier Proteins, Models, Molecular, Molecular Sequence Data, Magnetic Resonance Spectroscopy, Proline, Protein Conformation, Protein Processing, Post-Translational, Virion, HIV-1, HIV Core Protein p24, Protein Structure, Secondary, Protein Structure, Tertiary, Peptidylprolyl Isomerase
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