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 Kolatkar, Maxey C M Chung

Research output: Contribution to journalArticle

10 Citations (Scopus)

Abstract

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
Volume424
Issue number1
DOIs
Publication statusPublished - 1 Apr 2004
Externally publishedYes

Fingerprint

C-Type Lectins
Venoms
Platelets
Platelet Aggregation
Trimeresurus
Dimers
Agglomeration
Static Electricity
Hydrophobic and Hydrophilic Interactions
Polyacrylamide Gel Electrophoresis
Carrier Proteins
Proteins
Molecular modeling
Blood Platelets
Molecular mass
Peptides
Electrostatics
Trimeresurus venoms
echicetin

Keywords

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

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Purpureotin : A novel di-dimeric C-type lectin-like protein from Trimeresurus purpureomaculatus venom is stabilized by noncovalent interactions. / Li, Xiaolei; Zheng, Lu; Kong, Chunguang; Kolatkar, Prasanna; Chung, Maxey C M.

In: Archives of Biochemistry and Biophysics, Vol. 424, No. 1, 01.04.2004, p. 53-62.

Research output: Contribution to journalArticle

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