1sb2
|
High resolution Structure determination of rhodocetin
OverviewOverview
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 StructureAbout this Structure
1SB2 is a Protein complex structure of sequences from Calloselasma rhodostoma. Full crystallographic information is available from OCA.
ReferenceReference
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 Wed Nov 21 02:14:23 2007