Please use this identifier to cite or link to this item:
Title: A novel dimer of a C-type lectin-like heterodimer from the venom of Calloselasma rhodostoma (Malayan pit viper)
Authors: Wang, R.
Kong, C.
Chung, M.C.M. 
Kolatkar, P.
Keywords: C-type lectin-like protein
Calloselasma rhodostoma
Molecular modeling
Platelet aggregation
Sequence homology
Issue Date: 2001
Citation: Wang, R., Kong, C., Chung, M.C.M., Kolatkar, P. (2001). A novel dimer of a C-type lectin-like heterodimer from the venom of Calloselasma rhodostoma (Malayan pit viper). FEBS Letters 508 (3) : 447-453. ScholarBank@NUS Repository.
Abstract: We have isolated a potent platelet aggregation inducer from the crude venom of Calloselasma rhodostoma (Malayan pit viper), termed rhodoaggretin, with a novel oligomeric structure consisting of a dimer of C-type lectin-like heterodimers. On the basis of its native molecular mass of 66 kDa, and a Mr of 30 kDa for its disulfide-linked αβ-heterodimer, we propose that rhodoaggretin exists as a (αβ)2 complex in the native state. We postulate that the di-dimer is stabilized by non-covalent interactions as well as by an intersubunit disulfide bridge between the two αβ-heterodimers. This conclusion is based on the following observations: (a) sodium dodecylsulfate-polyacrylamide gel electrophoresis (SDS-PAGE) of the non-reduced rhodoaggretin gave a major 28 and a minor 52 kDa band. (b) Prior treatment of rhodoaggretin with a limited amount of 2-mercaptoethanol (2-ME; 0.1%) resulted in the complete abolishment of the 52 kDa band in SDS-PAGE. (c) Two-dimensional SDS-PAGE in the presence of 3% 2-ME showed that both the 28 and 52 kDa bands gave two bands each with Mrs of 18 (α-subunit) and 15 (β-subunit) kDa. (d) Mass spectrometric analyses showed that purified rhodoaggretin had a Mr of 30 155.39±3.25 Da while its s-pyridylethylated α- and β-subunits had Mrs of 16 535.62±2.98 and 15 209.89±1.61 Da respectively. These molecular weight data suggested the presence of 15 cysteinyl residues in rhodoaggretin as compared to the 14 that are reported for the heterodimeric C-type lectin-like proteins. This extra cysteinyl residue is a candidate for the formation of the intersubunit disulfide bond in the (αβ)2 complex. (e) Homology structural modeling studies showed that the extra cysteinyl residue can indeed form a disulfide bond that covalently links the two αβ-heterodimers as proposed above. © 2001 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.
Source Title: FEBS Letters
ISSN: 00145793
DOI: 10.1016/S0014-5793(01)03071-X
Appears in Collections:Staff Publications

Show full item record
Files in This Item:
There are no files associated with this item.


checked on Apr 1, 2020


checked on Jul 2, 2019

Page view(s)

checked on Mar 31, 2020

Google ScholarTM



Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.