Please use this identifier to cite or link to this item: https://doi.org/10.1110/ps.04945605
Title: Structure of rhodocetin reveals noncovalently bound heterodimer interface
Authors: Paaventhan, P. 
Kong, C.
Joseph, J.S.
Chung, M.C.M. 
Kolatkar, P.R. 
Keywords: C-type lectin-like protein
Calloselasma rhodostoma
Domain swapping
Heterodimer
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
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