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Protein Science (2008), 17:939-944. Published by Cold Spring Harbor Laboratory Press. Copyright © 2008 The Protein Society
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PROTEIN STRUCTURE REPORT

Conformational gating of dimannose binding to the antiviral protein cyanovirin revealed from the crystal structure at 1.35 Å resolution

Raimund Fromme, Zivile Katiliene, Petra Fromme, and Giovanna Ghirlanda

Department of Chemistry and Biochemistry, Arizona State University, Tempe, Arizona 85287-1604, USA

(RECEIVED January 28, 2008; FINAL REVISION February 29, 2008; ACCEPTED March 3, 2008)

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 Å 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 Å 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.

Keywords: cyanovirin; lectins; sugar binding; antiviral protein; X-ray structure analysis


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