PDBsum entry 4xfx

Viral protein

PDB id: 4xfx

Contents

Protein chain

216 a.a.

Metals

_CL ×2

IOD ×7

Waters ×75

PDB id:

4xfx

Name:

Viral protein

Title:

Structure of the native full-length HIV-1 capsid protein

Structure:

HIV-1 capsid protein. Chain: a. Synonym: pr55gag. Engineered: yes

Source:

Human immunodeficiency virus type 1 group m subtype b (isolate ny5). HIV-1. Organism_taxid: 11698. Strain: isolate ny5. Gene: gag. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

2.43Å R-factor: 0.223 R-free: 0.249

Authors:

A.T.Gres,K.A.Kirby,S.G.Sarafianos

Key ref:

A.T.Gres et al. (2015). STRUCTURAL VIROLOGY. X-ray crystal structures of native HIV-1 capsid protein reveal conformational variability. Science, 349, 99. PubMed id: 26044298 DOI: 10.1126/science.aaa5936

Date:

29-Dec-14 Release date: 10-Jun-15

Protein chain

P12493  (GAG_HV1N5) -  Gag polyprotein from Human immunodeficiency virus type 1 group M subtype B (isolate NY5)

Seq: 500 a.a.

Struc: 216 a.a.*

* PDB and UniProt seqs differ at 3 residue positions (black crosses)

DOI no: 10.1126/science.aaa5936

Science 349:99 (2015)

PubMed id: 26044298

STRUCTURAL VIROLOGY. X-ray crystal structures of native HIV-1 capsid protein reveal conformational variability.

A.T.Gres, K.A.Kirby, V.N.KewalRamani, J.J.Tanner, O.Pornillos, S.G.Sarafianos.

ABSTRACT

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 sixfold symmetry within hexamers (intrahexamer) and threefold and twofold symmetry between neighboring hexamers (interhexamer). 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 interhexamer interfaces, highlighting an inherent structural variability. A CA-targeting antiviral affects capsid stability by binding across CA molecules and subtly altering interhexamer 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.