Structure of rhodocetin reveals noncovalently bound heterodimer interface

Palasingam Paaventhan, Chunguang Kong, Jeremiah S. Joseph, Max C.M. Chung, Prasanna R. Kolatkar

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20 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)169-175
Number of pages7
JournalProtein Science
Issue number1
Publication statusPublished - 1 Jan 2005



  • C-type lectin-like protein
  • Calloselasma rhodostoma
  • Domain swapping
  • Heterodimer
  • Platelet aggregation inhibitor

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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