4xfz

From Proteopedia

Structure of the native full-length HIV-1 capsid protein in complex with PF-3450074 (PF74)

PDB ID 4xfz

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Structural highlights

4xfz is a 1 chain structure with sequence from Human immunodeficiency virus type 1 (NEW YORK-5 ISOLATE). Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.7Å
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GAG_HV1N5 Matrix protein p17 targets Gag and Gag-Pol polyproteins to the plasma membrane via a multipartite membrane binding signal, that includes its myristoylated N-terminus. Also mediates nuclear localization of the preintegration complex. Implicated in the release from host cell mediated by Vpu. Capsid protein p24 forms the conical core of the virus that encapsulates the genomic RNA-nucleocapsid complex. Nucleocapsid protein p7 encapsulates and protects viral dimeric unspliced (genomic) RNA. Binds these RNAs through its zinc fingers. p6-gag plays a role in budding of the assembled particle by interacting with the host class E VPS proteins TSG101 and PDCD6IP/AIP1 (By similarity).

Publication Abstract from PubMed

The detailed molecular interactions between native HIV-1 capsid protein (CA) hexamers that shield the viral genome and proteins have been elusive. We report crystal structures describing interactions between CA monomers related by 6-fold symmetry within hexamers (intra-hexamer), and 3-fold and 2-fold symmetry between neighboring hexamers (inter-hexamer). The structures describe how CA builds hexagonal lattices, the foundation of mature capsids. Lattice structure depends on an adaptable hydration layer modulating interactions among CA molecules. Disruption of this layer alters inter-hexamer interfaces, highlighting an inherent structural variability. A CA-targeting antiviral affects capsid stability by binding across CA molecules and altering inter-hexamer interfaces remote to the ligand-binding site. Inherent structural plasticity, hydration layer rearrangement, and effector-binding affect capsid stability and have functional implications for the retroviral life-cycle.

X-ray crystal structures of native HIV-1 capsid protein reveal conformational variability.,Gres AT, Kirby KA, KewalRamani VN, Tanner JJ, Pornillos O, Sarafianos SG Science. 2015 Jun 4. pii: aaa5936. PMID:26044298^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Gres AT, Kirby KA, KewalRamani VN, Tanner JJ, Pornillos O, Sarafianos SG. X-ray crystal structures of native HIV-1 capsid protein reveal conformational variability. Science. 2015 Jun 4. pii: aaa5936. PMID:26044298 doi:http://dx.doi.org/10.1126/science.aaa5936