PDBsum entry 5jyn

Viral protein

PDB id: 5jyn

Contents

Protein chains

40 a.a.

PDB id:

5jyn

Name:

Viral protein

Title:

Structure of the transmembrane domain of HIV-1 gp41 in bicelle

Structure:

Envelope glycoprotein gp160. Chain: a, b, c. Fragment: gp41 domain residues 670-709. Engineered: yes

Source:

Human immunodeficiency virus 1. Organism_taxid: 11676. Gene: env. Expressed in: escherichia coli. Expression_system_taxid: 469008.

NMR struc:

15 models

Authors:

J.Dev,Q.Fu,D.Park,B.Chen,J.J.Chou

Key ref:

J.Dev et al. (2016). Structural basis for membrane anchoring of HIV-1 envelope spike. Science, 353, 172-175. PubMed id: 27338706 DOI: 10.1126/science.aaf7066

Date:

14-May-16 Release date: 29-Jun-16

Protein chains

Q74849  (Q74849_HV1) -  Envelope glycoprotein gp160 (Fragment) from Human immunodeficiency virus type 1

Seq: 849 a.a.

Struc: 40 a.a.

DOI no: 10.1126/science.aaf7066

Science 353:172-175 (2016)

PubMed id: 27338706

Structural basis for membrane anchoring of HIV-1 envelope spike.

J.Dev, D.Park, Q.Fu, J.Chen, H.J.Ha, F.Ghantous, T.Herrmann, W.Chang, Z.Liu, G.Frey, M.S.Seaman, B.Chen, J.J.Chou.

ABSTRACT

HIV-1 envelope spike (Env) is a type I membrane protein that mediates viral entry. We used nuclear magnetic resonance to determine an atomic structure of the transmembrane (TM) domain of HIV-1 Env reconstituted in bicelles that mimic a lipid bilayer. The TM forms a well-ordered trimer that protects a conserved membrane-embedded arginine. An amino-terminal coiled-coil and a carboxyl-terminal hydrophilic core stabilize the trimer. Individual mutations of conserved residues did not disrupt the TM trimer and minimally affected membrane fusion and infectivity. Major changes in the hydrophilic core, however, altered the antibody sensitivity of Env. These results show how a TM domain anchors, stabilizes, and modulates a viral envelope spike and suggest that its influence on Env conformation is an important consideration for HIV-1 immunogen design.