1SZT

ATOMIC STRUCTURE OF A THERMOSTABLE SUBDOMAIN OF HIV-1 GP41

Summary for 1SZT

• Entry DOI: 10.2210/pdb1szt/pdb
• Descriptor: HIV-1 ENVELOPE GLYCOPROTEIN GP41 (2 entities in total)
• Functional Keywords: coat protein, hiv-1 envelope glycoprotein, viral protein
• Biological source: Human immunodeficiency virus 1
• Cellular location: Transmembrane protein gp41: Virion membrane; Single-pass type I membrane protein. Surface protein gp120: Virion membrane; Peripheral membrane protein: P04582
• Total number of polymer chains: 1
• Total formula weight: 7879.75

Authors

Tan, K.,Lu, M.,Wang, J.-H. (deposition date: 1997-07-28, release date: 1997-12-24, Last modification date: 2024-02-14)

Primary citation

Tan, K.,Liu, J.,Wang, J.,Shen, S.,Lu, M.
Atomic structure of a thermostable subdomain of HIV-1 gp41.
Proc.Natl.Acad.Sci.USA, 94:12303-12308, 1997

PubMed Abstract: Infection by HIV-1 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 viral-cell membrane fusion. A soluble, alpha-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.

PubMed: 9356444
DOI: 10.1073/pnas.94.23.12303

Experimental method

X-RAY DIFFRACTION (2.4 Å)