3lhc
Crystal structure of cyanovirin-n swapping domain b mutant
Structural highlights
FunctionCVN_NOSEL Mannose-binding lectin.[1] [2] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedCyanovirin-N (CV-N) is a two-domain, cyanobacterial protein that inhibits human immunodeficiency virus (HIV) at nanomolar concentrations by binding to high mannose sugars on the HIV envelope glycoprotein gp120. The wild type protein can exist as a monomer or a domain-swapped dimer with the monomer and dimer containing two or four sugar binding sites, respectively, one on each domain. Here we demonstrate that monomeric, single binding site mutants are completely inactive and that a single site, whether located on domain A or B, is insufficient to impart the antiviral activity. Linking inactive, monomeric proteins in a head-to-head fashion by an intermolecular disulfide bond or by creating an exclusively domain-swapped dimer via a hinge residue deletion restored antiviral activity to levels similar to that of wild type CV-N. These findings demonstrate unequivocally that multisite binding by CV-N type lectins is necessary for viral inhibition. Anti-HIV activity of defective cyanovirin-N mutants is restored by dimerization.,Matei E, Zheng A, Furey W, Rose J, Aiken C, Gronenborn AM J Biol Chem. 2010 Apr 23;285(17):13057-65. Epub 2010 Feb 10. PMID:20147291[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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