2RDK : Five site mutated Cyanovirin-N with Mannose dimer bound

Dataset

Description

Experimental Technique/Method:X-RAY DIFFRACTION
Resolution:1.35
Classification:ANTIVIRAL PROTEIN
Release Date:2008-05-06
Deposition Date:2007-09-24
Revision Date:2011-07-13
Molecular Weight:24618.81
Macromolecule Type:Protein
Residue Count:218
Atom Site Count:1585
DOI:10.2210/pdb2rdk/pdb

Abstract:
Cyanovirin (CV-N) is a small lectin with potent HIV neutralization activity, which could be exploited for a mucosal defense against HIV infection. The wild-type (wt) protein binds with high affinity to mannose-rich oligosaccharides on the surface of gp120 through two quasi-symmetric sites, located in domains A and B. We recently reported on a mutant of CV-N that contained a single functional mannose-binding site, domain B, showing that multivalent binding to oligomannosides is necessary for antiviral activity. The structure of the complex with dimannose determined at 1.8 A resolution revealed a different conformation of the binding site than previously observed in the NMR structure of wt CV-N. Here, we present the 1.35 A resolution structure of the complex, which traps three different binding conformations of the site and provides experimental support for a locking and gating mechanism in the nanoscale time regime observed by molecular dynamics simulations.
Date made availableMay 6 2008
PublisherRCSB-PDB

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