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|Title:||A novel dimer of a C-type lectin-like heterodimer from the venom of Calloselasma rhodostoma (Malayan pit viper)|
|Keywords:||C-type lectin-like protein|
|Source:||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. https://doi.org/10.1016/S0014-5793(01)03071-X|
|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|
|Appears in Collections:||Staff Publications|
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