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2BUO

HIV-1 capsid C-terminal domain in complex with an inhibitor of particle assembly

Summary for 2BUO
Entry DOI10.2210/pdb2buo/pdb
Related1L6N 1M9C 1M9D 1M9E 1M9F 1M9X 1M9Y
DescriptorHIV-1 CAPSID PROTEIN, INHIBITOR OF CAPSID ASSEMBLY, ACETIC ACID, ... (4 entities in total)
Functional Keywordsviral protein/peptide, hiv, capsid, inhibitor, assembly, polyprotein, complex (viral protein-peptide), viral protein-peptide complex
Biological sourceHUMAN IMMUNODEFICIENCY VIRUS 1 (HIV-1)
More
Cellular locationHost cytoplasm . Host nucleus . Matrix protein p17: Virion . Virion : Q72497
Total number of polymer chains2
Total formula weight11036.54
Authors
Ternois, F.,Sticht, J.,Duquerroy, S.,Krausslich, H.-G.,Rey, F.A. (deposition date: 2005-06-17, release date: 2005-07-21, Last modification date: 2023-12-13)
Primary citationTernois, F.,Sticht, J.,Duquerroy, S.,Krausslich, H.-G.,Rey, F.A.
The HIV-1 Capsid Protein C-Terminal Domain in Complex with a Virus Assembly Inhibitor
Nat.Struct.Mol.Biol., 12:678-, 2005
Cited by
PubMed Abstract: Immature HIV particles bud from infected cells after assembly at the cytoplasmic side of cellular membranes. This assembly is driven by interactions between Gag polyproteins. Mature particles, each containing a characteristic conical core, are later generated by proteolytic maturation of Gag in the virion. The C-terminal domain of the HIV-1 capsid protein (C-CA) has been shown to contain oligomerization determinants essential for particle assembly. Here we report the 1.7-A-resolution crystal structure of C-CA in complex with a peptide capable of inhibiting immature- and mature-like particle assembly in vitro. The peptide inserts as an amphipathic alpha-helix into a conserved hydrophobic groove of C-CA, resulting in formation of a compact five-helix bundle with altered dimeric interactions. This structure thus reveals the details of an allosteric site in the HIV capsid protein that can be targeted for antiviral therapy.
PubMed: 16041386
DOI: 10.1038/NSMB967
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.7 Å)
Structure validation

238895

数据于2025-07-16公开中

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