Structure of rhodocetin reveals noncovalently bound heterodimer interface

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

Research output: Contribution to journalArticle

20 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)169-175
Number of pages7
JournalProtein Science
Volume14
Issue number1
DOIs
Publication statusPublished - 1 Jan 2005
Externally publishedYes

Fingerprint

Disulfides
Dimers
Crotalid Venoms
Lectins
Collagen
Agglomeration
Molecules
rhodocetin
Proteins

Keywords

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

ASJC Scopus subject areas

  • Biochemistry

Cite this

Structure of rhodocetin reveals noncovalently bound heterodimer interface. / Paaventhan, Palasingam; Kong, Chunguang; Joseph, Jeremiah S.; Chung, Max C M; Kolatkar, Prasanna.

In: Protein Science, Vol. 14, No. 1, 01.01.2005, p. 169-175.

Research output: Contribution to journalArticle

Paaventhan, Palasingam ; Kong, Chunguang ; Joseph, Jeremiah S. ; Chung, Max C M ; Kolatkar, Prasanna. / Structure of rhodocetin reveals noncovalently bound heterodimer interface. In: Protein Science. 2005 ; Vol. 14, No. 1. pp. 169-175.
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