Please use this identifier to cite or link to this item: https://doi.org/10.1016/j.abb.2004.01.015
Title: Purpureotin: A novel di-dimeric C-type lectin-like protein from Trimeresurus purpureomaculatus venom is stabilized by noncovalent interactions
Authors: Li, X.
Zheng, L. 
Kong, C.
Kolatkar, P.R.
Chung, M.C.M.
Keywords: C-type lectin-like protein
Molecular modeling
Platelet aggregation
Purpureotin
Sequence identity
Trimeresurus purpureomaculatus
Issue Date: 1-Apr-2004
Citation: Li, X., Zheng, L., Kong, C., Kolatkar, P.R., Chung, M.C.M. (2004-04-01). Purpureotin: A novel di-dimeric C-type lectin-like protein from Trimeresurus purpureomaculatus venom is stabilized by noncovalent interactions. Archives of Biochemistry and Biophysics 424 (1) : 53-62. ScholarBank@NUS Repository. https://doi.org/10.1016/j.abb.2004.01.015
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. © 2004 Elsevier Inc. All rights reserved.
Source Title: Archives of Biochemistry and Biophysics
URI: http://scholarbank.nus.edu.sg/handle/10635/111047
ISSN: 00039861
DOI: 10.1016/j.abb.2004.01.015
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