PDBsum entry 6obh

Viral protein

PDB id: 6obh

Contents

Protein chains

220 a.a.

214 a.a.

Metals

_NA ×6

Waters ×3

PDB id:

6obh

Name:

Viral protein

Title:

Structure of HIV-1 ca 1/2-hexamer

Structure:

Ca. Chain: a, d. Fragment: unp residues 107-337. Engineered: yes. Mutation: yes. Ca. Chain: b, e. Fragment: unp residues 133-363. Engineered: yes.

Source:

Human immunodeficiency virus 1. HIV-1. Organism_taxid: 11676. Gene: gag. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Resolution:

2.96Å R-factor: 0.211 R-free: 0.265

Authors:

B.J.Summers,Y.Xiong

Key ref:

B.J.Summers et al. (2019). Modular HIV-1 Capsid Assemblies Reveal Diverse Host-Capsid Recognition Mechanisms. Cell Host Microbe, 26, 203. PubMed id: 31415753

Date:

20-Mar-19 Release date: 28-Aug-19

Protein chains

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

Seq: 500 a.a.

Struc: 220 a.a.*

Protein chains

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

Seq: 500 a.a.

Struc: 214 a.a.*

* PDB and UniProt seqs differ at 7 residue positions (black crosses)

Cell Host Microbe 26:203 (2019)

PubMed id: 31415753

Modular HIV-1 Capsid Assemblies Reveal Diverse Host-Capsid Recognition Mechanisms.

B.J.Summers, K.M.Digianantonio, S.S.Smaga, P.T.Huang, K.Zhou, E.E.Gerber, W.Wang, Y.Xiong.

ABSTRACT

The HIV-1 capsid is an ordered protein shell that houses the viral genome during early infection. Its expansive surface consists of an ordered and interfacing array of capsid protein hexamers and pentamers that are recognized by numerous cellular proteins. Many of these proteins recognize specific, assembled capsid interfaces not present in unassembled capsid subunits. We used protein-engineering tools to capture diverse capsid assembly intermediates. We built a repertoire of capsid assemblies (ranging from two to 42 capsid protein molecules) that recreate the various surfaces in infectious capsids. These assemblies reveal unique capsid-targeting mechanisms for each of the anti-HIV factors, TRIMCyp, MxB, and TRIM5α, linked to inhibition of virus uncoating and nuclear entry, as well as the HIV-1 cofactor FEZ1 that facilitates virus intracellular trafficking. This capsid assembly repertoire enables elucidation of capsid recognition modes by known capsid-interacting factors, identification of new capsid-interacting factors, and potentially, development of capsid-targeting therapeutics.