Atomic structure of a thermostable subdomain of HIV-1 gp41

Kemin Tan, Jin Huan Liu, Jia Huai Wang, Steven Shen, Min Lu

Research output: Contribution to journalArticlepeer-review

519 Scopus citations

Abstract

Infection by HIV-I involves the fusion of viral and cellular membranes with subsequent transfer of viral genetic material into the cell. The HIV-1 envelope glycoprotein that mediates fusion consists of the surface subunit gp120 and the transmembrane subunit gp41.gp120 directs virion attachment to the cell-surface receptors. and gp41 then promotes vital-cell membrane fusion. A soluble, α-helical, trimeric complex within gp41 composed of N- terminal and C-terminal extraviral segments has been proposed to represent the core of the fusion-active conformation of the HIV-1 envelope. A thermostable subdomain denoted N34(L6)C28 can be formed by the N-34 and C-28 peptides connected by a flexible linker in place of the disulfide-bonded loop region. Three-dimensional structure of N34(L6)C28 reveals that three molecules fold into a six-stranded helical bundle. Three N-terminal helices within the bundle form a central, parallel, trimeric coiled coil, whereas three C-terminal helices pack in the reverse direction into three hydrophobic grooves on the surface of the N-terminal trimer. This thermostable subdomain displays the salient features of the core structure of the isolated gp41 subunit and thus provides a possible target for therapeutics designed selectively to block HIV-1 entry.

Original languageEnglish (US)
Pages (from-to)12303-12308
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume94
Issue number23
DOIs
StatePublished - Nov 11 1997

ASJC Scopus subject areas

  • General

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