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|Title:||Structure of rhodocetin reveals noncovalently bound heterodimer interface||Authors:||Paaventhan, P.
|Keywords:||C-type lectin-like protein
Platelet aggregation inhibitor
|Issue Date:||Jan-2005||Citation:||Paaventhan, P., Kong, C., Joseph, J.S., Chung, M.C.M., Kolatkar, P.R. (2005-01). Structure of rhodocetin reveals noncovalently bound heterodimer interface. Protein Science 14 (1) : 169-175. ScholarBank@NUS Repository. https://doi.org/10.1110/ps.04945605||Abstract:||Rhodocetin is a unique heterodimer consisting of α- and β-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 Ca2+- dependent lectin-like proteins. We report here the 1.9 Å resolution structure of rhodocetin, which reveals the compensatory interactions that occur in the absence of the disulfide bridge to preserve activity.||Source Title:||Protein Science||URI:||http://scholarbank.nus.edu.sg/handle/10635/130407||ISSN:||09618368||DOI:||10.1110/ps.04945605|
|Appears in Collections:||Staff Publications|
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