Structure of rhodocetin reveals noncovalently bound heterodimer interface

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
Appears in Collections:	Staff Publications

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