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Structure of rhodocetin reveals noncovalently bound heterodimer interface
Author(s) -
Paaventhan Palasingam,
Kong Chunguang,
Joseph Jeremiah S.,
Chung Max C.M.,
Kolatkar Prasanna R.
Publication year - 2005
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.04945605
Subject(s) - interface (matter) , chemistry , crystallography , biophysics , physics , biology , molecule , organic chemistry , gibbs isotherm
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 Ca 2+ ‐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.

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