2jmv
From Proteopedia
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[[Image:2jmv.jpg|left|200px]] | [[Image:2jmv.jpg|left|200px]] | ||
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'''Solution structure of scytovirin refined against residual dipolar couplings''' | '''Solution structure of scytovirin refined against residual dipolar couplings''' | ||
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==About this Structure== | ==About this Structure== | ||
| - | + | Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JMV OCA]. | |
==Reference== | ==Reference== | ||
The novel fold of scytovirin reveals a new twist for antiviral entry inhibitors., McFeeters RL, Xiong C, O'Keefe BR, Bokesch HR, McMahon JB, Ratner DM, Castelli R, Seeberger PH, Byrd RA, J Mol Biol. 2007 Jun 1;369(2):451-61. Epub 2007 Mar 20. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17434526 17434526] | The novel fold of scytovirin reveals a new twist for antiviral entry inhibitors., McFeeters RL, Xiong C, O'Keefe BR, Bokesch HR, McMahon JB, Ratner DM, Castelli R, Seeberger PH, Byrd RA, J Mol Biol. 2007 Jun 1;369(2):451-61. Epub 2007 Mar 20. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17434526 17434526] | ||
| - | [[Category: Protein complex]] | ||
| - | [[Category: Scytonema varium]] | ||
[[Category: Byrd, R A.]] | [[Category: Byrd, R A.]] | ||
[[Category: McFeeters, R L.]] | [[Category: McFeeters, R L.]] | ||
| - | [[Category: | + | [[Category: Protein]] |
| - | [[Category: | + | [[Category: Sugar binding protein]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 09:02:56 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 06:02, 4 May 2008
Solution structure of scytovirin refined against residual dipolar couplings
Overview
The solution structure of the potent 95 residue anti-HIV protein scytovirin has been determined and two carbohydrate-binding sites have been identified. This unique protein, containing five structurally important disulfide bonds, demonstrates a novel fold with no elements of extended regular secondary structure. Scytovirin contains two 39 residue sequence repeats, differing in only three amino acid residues, and each repeat has primary sequence similarity to chitin binding proteins. Both sequence repeats form similarly structured domains, with the exception of one region. The result is two carbohydrate-binding sites with substantially different affinities. The unusual fold clusters aromatic residues in both sites, suggesting a binding mechanism similar to other known hevein-like carbohydrate-binding proteins but differing in carbohydrate specificity. Scytovirin, originally isolated from the cyanobacterium Scytonema varium, holds potential as an HIV entry inhibitor for both therapeutic and prophylactic anti-HIV applications. The high-resolution structural studies reported are an important initial step in unlocking the therapeutic potential of scytovirin.
About this Structure
Full crystallographic information is available from OCA.
Reference
The novel fold of scytovirin reveals a new twist for antiviral entry inhibitors., McFeeters RL, Xiong C, O'Keefe BR, Bokesch HR, McMahon JB, Ratner DM, Castelli R, Seeberger PH, Byrd RA, J Mol Biol. 2007 Jun 1;369(2):451-61. Epub 2007 Mar 20. PMID:17434526 Page seeded by OCA on Sun May 4 09:02:56 2008
