1jek
From Proteopedia
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Visna TM CORE STRUCTURE
Overview
Structural studies of viral membrane fusion proteins suggest that a, "trimer-of-hairpins" motif plays a critical role in the membrane fusion, process of many enveloped viruses. In this motif, a coiled coil (formed by, homotrimeric association of the N-terminal regions of the protein) is, surrounded by three C-terminal regions that pack against the coiled coil, in an oblique antiparallel manner. The resulting trimer-of-hairpins, structure serves to bring the viral and cellular membranes together for, fusion. learncoil-vmf, a computational program developed to recognize, coiled coil-like regions that form the trimer-of-hairpins motif, predicts, these regions in the membrane fusion protein of the Visna virus. Peptides, corresponding to the computationally identified sequences were, synthesized, and the soluble core of the Visna membrane fusion protein was, reconstituted in solution. Its crystal structure at 1.5-A resolution, demonstrates that a trimer-of-hairpins structure is formed. Remarkably, despite less than 23% sequence identity, the ectodomains in Visna and, HIV-1 envelope glycoproteins show detailed structural conservation, especially within the area of a hydrophobic pocket in the central coiled, coil currently being targeted for the development of new anti-HIV drugs.
About this Structure
1JEK is a Protein complex structure of sequences from [1] with ACE and NH2 as ligands. Full crystallographic information is available from OCA.
Reference
The trimer-of-hairpins motif in membrane fusion: Visna virus., Malashkevich VN, Singh M, Kim PS, Proc Natl Acad Sci U S A. 2001 Jul 17;98(15):8502-6. Epub 2001 Jul 10. PMID:11447278
Page seeded by OCA on Thu Nov 8 14:12:22 2007
Categories: Protein complex | Kim, P.S. | Malashkevich, V.N. | Singh, M. | ACE | NH2 | Envelope glycoprotein | Gp41 | Hiv | Retrovirus | Siv
