1AIK

HIV GP41 CORE STRUCTURE

Summary for 1AIK

• Entry DOI: 10.2210/pdb1aik/pdb
• Descriptor: HIV-1 GP41 GLYCOPROTEIN (3 entities in total)
• Functional Keywords: hiv, gp41, envelope glycoprotein, retrovirus, viral protein
• Biological source: HIV-1 M:B_HXB2R; More
• Cellular location: Transmembrane protein gp41: Virion membrane; Single-pass type I membrane protein. Surface protein gp120: Virion membrane; Peripheral membrane protein: P04578 P04578
• Total number of polymer chains: 2
• Total formula weight: 8430.46

Authors

Chan, D.C.,Fass, D.,Berger, J.M.,Kim, P.S. (deposition date: 1997-04-20, release date: 1997-06-16, Last modification date: 2024-10-16)

Primary citation

Chan, D.C.,Fass, D.,Berger, J.M.,Kim, P.S.
Core structure of gp41 from the HIV envelope glycoprotein.
Cell(Cambridge,Mass.), 89:263-273, 1997

PubMed Abstract: The envelope glycoprotein of human immunodeficiency virus type 1 (HIV-1) consists of a complex of gp120 and gp41. gp120 determines viral tropism by binding to target-cell receptors, while gp41 mediates fusion between viral and cellular membranes. Previous studies identified an alpha-helical domain within gp41 composed of a trimer of two interacting peptides. The crystal structure of this complex, composed of the peptides N36 and C34, is a six-helical bundle. Three N36 helices form an interior, parallel coiled-coil trimer, while three C34 helices pack in an oblique, antiparallel manner into highly conserved, hydrophobic grooves on the surface of this trimer. This structure shows striking similarity to the low-pH-induced conformation of influenza hemagglutinin and likely represents the core of fusion-active gp41. Avenues for the design/discovery of small-molecule inhibitors of HIV infection are directly suggested by this structure.

PubMed: 9108481
DOI: 10.1016/S0092-8674(00)80205-6

Experimental method

X-RAY DIFFRACTION (2 Å)