2SIV

SIV GP41 CORE STRUCTURE

Summary for 2SIV

• Entry DOI: 10.2210/pdb2siv/pdb
• Descriptor: SIV GP41 GLYCOPROTEIN (3 entities in total)
• Functional Keywords: envelope glycoprotein, retrovirus, hiv, siv, gp41, coat protein
• Biological source: Simian immunodeficiency virus; More
• Total number of polymer chains: 6
• Total formula weight: 25585.99

Authors

Malashkevich, V.N.,Chan, D.C.,Chutkowski, C.T.,Kim, P.S. (deposition date: 1998-06-17, release date: 1998-08-19, Last modification date: 2024-10-23)

Primary citation

Malashkevich, V.N.,Chan, D.C.,Chutkowski, C.T.,Kim, P.S.
Crystal structure of the simian immunodeficiency virus (SIV) gp41 core: conserved helical interactions underlie the broad inhibitory activity of gp41 peptides.
Proc.Natl.Acad.Sci.USA, 95:9134-9139, 1998

PubMed Abstract: The gp41 subunit of the envelope protein complex from human and simian immunodeficiency viruses (HIV and SIV) mediates membrane fusion during viral entry. The crystal structure of the HIV-1 gp41 ectodomain core in its proposed fusion-active state is a six-helix bundle. Here we have reconstituted the core of the SIV gp41 ectodomain with two synthetic peptides called SIV N36 and SIV C34, which form a highly helical trimer of heterodimers. The 2.2 A resolution crystal structure of this SIV N36/C34 complex is very similar to the analogous structure in HIV-1 gp41. In both structures, three N36 helices form a central trimeric coiled coil. Three C34 helices pack in an antiparallel orientation into highly conserved, hydrophobic grooves along the surface of this coiled coil. The conserved nature of the N36-C34 interface suggests that the HIV-1 and SIV peptides are functionally interchangeable. Indeed, a heterotypic complex between HIV-1 N36 and SIV C34 peptides is highly helical and stable. Moreover, as with HIV-1 C34, the SIV C34 peptide is a potent inhibitor of HIV-1 infection. These results identify conserved packing interactions between the N and C helices of gp41 and have implications for the development of C peptide analogs with broad inhibitory activity.

PubMed: 9689046
DOI: 10.1073/pnas.95.16.9134

Experimental method

X-RAY DIFFRACTION (2.2 Å)