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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.