Solution Structure of a Circular-permuted Variant of the Potent HIV-inactivating Protein Cyanovirin-N: Structural Basis for Protein Stability and Oligosaccharide Interaction-Reference-Cited by-同舟云学术

Solution Structure of a Circular-permuted Variant of the Potent HIV-inactivating Protein Cyanovirin-N: Structural Basis for Protein Stability and Oligosaccharide Interaction

Published:2003-01 Issue:1 Volume:325 Page:211-223
ISSN:0022-2836
Container-title:Journal of Molecular Biology
language:en
Short-container-title:Journal of Molecular Biology

Author:

Barrientos Laura G,Louis John M,Ratner Daniel M,Seeberger Peter H,Gronenborn Angela M

Publisher

Elsevier BV

Subject

Molecular Biology,Structural Biology

Reference32 articles.

1. Discovery of cyanovirin-N, a novel human immunodeficiency virus-inactivating protein that binds viral surface envelope glycoprotein gp120: potential applications to microbicide development;Boyd;Antimicrob. Agents Chemother.,1997

2. Multiple antiviral activities of cyanovirin-N: blocking of human immunodeficiency virus type 1 gp120 interaction with CD4 and coreceptor and inhibition of diverse enveloped viruses;Dey;J. Virol.,2000

3. Cyanovirin-N defines a new class of antiviral agent targeting N-linked, high-mannose glycans in an oligosaccharide-specific manner;Bolmstedt;Mol. Pharmacol.,2001

4. Selective interactions of the human immunodeficiency virus-inactivating protein cyanovirin-N with high-mannose oligosaccharides on gp120 and other glycoproteins;Shenoy;J. Pharmacol. Expt. Ther.,2001

5. Multisite and multivalent binding between cyanovirin-N and branched oligomannosides: calorimetric and NMR characterization;Shenoy;Chem. Biol.,2002

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