2jnr

From Proteopedia

Revision as of 13:21, 23 January 2008

Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide

Overview

A variety of molecules in human blood have been implicated in the, inhibition of HIV-1. However, it remained elusive which circulating, natural compounds are most effective in controlling viral replication in, vivo. To identify natural HIV-1 inhibitors we screened a comprehensive, peptide library generated from human hemofiltrate. The most potent, fraction contained a 20-residue peptide, designated VIRUS-INHIBITORY, PEPTIDE (VIRIP), corresponding to the C-proximal region of, alpha1-antitrypsin, the most abundant circulating serine protease, inhibitor. We found that VIRIP inhibits a wide variety of HIV-1 strains, including those resistant to current antiretroviral drugs. Further, analysis demonstrated that VIRIP blocks HIV-1 entry by interacting with, the gp41 fusion peptide and showed that a few amino acid changes increase, its antiretroviral potency by two orders of magnitude. Thus, as a highly, specific natural inhibitor of the HIV-1 gp41 fusion peptide, VIRIP may, lead to the development of another class of antiretroviral drugs.

About this Structure

2JNR is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.

Reference

Discovery and Optimization of a Natural HIV-1 Entry Inhibitor Targeting the gp41 Fusion Peptide., Munch J, Standker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pohlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F, Cell. 2007 Apr 20;129(2):263-75. PMID:17448989

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