1sb2

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{{STRUCTURE_1sb2| PDB=1sb2 | SCENE= }}
{{STRUCTURE_1sb2| PDB=1sb2 | SCENE= }}
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'''High resolution Structure determination of rhodocetin'''
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===High resolution Structure determination of rhodocetin===
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==Overview==
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Rhodocetin is a unique heterodimer consisting of alpha- and beta-subunits of 133 and 129 residues, respectively. The molecule, purified from the crude venom of the Malayan pit viper, Calloselasma rhodostoma, functions as an inhibitor of collagen-induced aggregation. Rhodocetin has been shown to have activity only when present as a dimer. The dimer is formed without an intersubunit disulfide bridge, unlike all the other Ca(2+)-dependent lectin-like proteins. We report here the 1.9 A resolution structure of rhodocetin, which reveals the compensatory interactions that occur in the absence of the disulfide bridge to preserve activity.
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{{ABSTRACT_PUBMED_15576563}}
==About this Structure==
==About this Structure==
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[[Category: C-type lectin]]
[[Category: C-type lectin]]
[[Category: Domain swapping]]
[[Category: Domain swapping]]
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Revision as of 00:42, 29 July 2008

Image:1sb2.png

Template:STRUCTURE 1sb2

High resolution Structure determination of rhodocetin

Template:ABSTRACT PUBMED 15576563

About this Structure

1SB2 is a Protein complex structure of sequences from Calloselasma rhodostoma. Full crystallographic information is available from OCA.

Reference

Structure of rhodocetin reveals noncovalently bound heterodimer interface., Paaventhan P, Kong C, Joseph JS, Chung MC, Kolatkar PR, Protein Sci. 2005 Jan;14(1):169-75. Epub 2004 Dec 2. PMID:15576563

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