1sb2
From Proteopedia
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'''High resolution Structure determination of rhodocetin''' | '''High resolution Structure determination of rhodocetin''' | ||
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[[Category: Kong, C G.]] | [[Category: Kong, C G.]] | ||
[[Category: Paaventhan, P.]] | [[Category: Paaventhan, P.]] | ||
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Revision as of 05:30, 3 May 2008
High resolution Structure determination of rhodocetin
Overview
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.
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 Page seeded by OCA on Sat May 3 08:29:59 2008
