2rdk

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{{STRUCTURE_2rdk| PDB=2rdk | SCENE= }}
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'''Five site mutated Cyanovirin-N with Mannose dimer bound'''
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===Five site mutated Cyanovirin-N with Mannose dimer bound===
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==Overview==
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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.
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==About this Structure==
==About this Structure==
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==Reference==
==Reference==
Conformational gating of dimannose binding to the antiviral protein cyanovirin revealed from the crystal structure at 1.35 A resolution., Fromme R, Katiliene Z, Fromme P, Ghirlanda G, Protein Sci. 2008 May;17(5):939-44. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18436959 18436959]
Conformational gating of dimannose binding to the antiviral protein cyanovirin revealed from the crystal structure at 1.35 A resolution., Fromme R, Katiliene Z, Fromme P, Ghirlanda G, Protein Sci. 2008 May;17(5):939-44. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18436959 18436959]
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A monovalent mutant of cyanovirin-N provides insight into the role of multiple interactions with gp120 for antiviral activity., Fromme R, Katiliene Z, Giomarelli B, Bogani F, Mc Mahon J, Mori T, Fromme P, Ghirlanda G, Biochemistry. 2007 Aug 14;46(32):9199-207. Epub 2007 Jul 18. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17636873 17636873]
[[Category: Nostoc ellipsosporum]]
[[Category: Nostoc ellipsosporum]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Sugar binding protein]]
[[Category: Sugar binding protein]]
[[Category: X-ray diffraction]]
[[Category: X-ray diffraction]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 7 08:43:10 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 05:51:18 2008''

Revision as of 02:51, 29 July 2008

Image:2rdk.png

Template:STRUCTURE 2rdk

Five site mutated Cyanovirin-N with Mannose dimer bound

Template:ABSTRACT PUBMED 18436959

About this Structure

2RDK is a Single protein structure of sequence from Nostoc ellipsosporum. Full crystallographic information is available from OCA.

Reference

Conformational gating of dimannose binding to the antiviral protein cyanovirin revealed from the crystal structure at 1.35 A resolution., Fromme R, Katiliene Z, Fromme P, Ghirlanda G, Protein Sci. 2008 May;17(5):939-44. PMID:18436959

A monovalent mutant of cyanovirin-N provides insight into the role of multiple interactions with gp120 for antiviral activity., Fromme R, Katiliene Z, Giomarelli B, Bogani F, Mc Mahon J, Mori T, Fromme P, Ghirlanda G, Biochemistry. 2007 Aug 14;46(32):9199-207. Epub 2007 Jul 18. PMID:17636873

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