Purpureotin: A novel di-dimeric C-type lectin-like protein from Trimeresurus purpureomaculatus venom is stabilized by noncovalent interactions

Xiaolei Li, Lu Zheng, Chunguang Kong, Prasanna R. Kolatkar, Maxey C.M. Chung

Research output: Contribution to journalArticle

10 Citations (Scopus)


Purpureotin, a novel di-dimeric C-type lectin-like protein (CLP) from Trimeresurus purpureomaculatus, was purified and sequenced. While its native molecular mass was determined to be 63kDa, purpureotin showed a single band of 30kDa on nonreducing SDS-PAGE and two polypeptide chains (16.0 and 14.5kDa) under reducing condition. These results were subsequently confirmed by mass spectrometric analyses. Based on these results, we postulate that purpureotin is a dimer of the α,β-heterodimer which is held together by noncovalent interactions. Molecular modeling studies indicate that a dimer of α,β-heterodimers can be formed where the α chains are held together by electrostatic charges and β chains via hydrophobic interactions. Functionally, purpureotin induced platelet aggregation without any cofactor in a dose-dependent manner. However, the platelet aggregation effect was blocked by echicetin. Therefore, purpureotin is assumed to be a GPIb-binding protein which binds to the same or a closely related GPIb site on platelets as echicetin.

Original languageEnglish
Pages (from-to)53-62
Number of pages10
JournalArchives of Biochemistry and Biophysics
Issue number1
Publication statusPublished - 1 Apr 2004



  • C-type lectin-like protein
  • Molecular modeling
  • Platelet aggregation
  • Purpureotin
  • Sequence identity
  • Trimeresurus purpureomaculatus

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology

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