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http://dspace.mediu.edu.my:8181/xmlui/handle/10261/3631| Title: | Snake venom disintegrins: novel dimeric disintegrins and structural diversification by disulphide bond engineering |
| Keywords: | Disintegrin Disulphide bond Evolution Protein sequence Snake venom protein |
| Publisher: | Biochemical Society |
| Description: | The final version of record is available at: http://www.biochemj.org/bj/default.htm We report the isolation and amino acid sequences of six novel dimeric disintegrins from the venoms of Vipera lebetina obtusa (VLO), V. berus (VB), V. ammodytes (VA), Echis ocellatus (EO) and Echis multisquamatus (EMS). Disintegrins VLO4, VB7, VA6 and EO4 displayed the RGD motif and inhibited the adhesion of K562 cells, expressing the integrin alpha5beta1 to immobilized fibronectin. A second group of dimeric disintegrins (VLO5 and EO5) had MLD and VGD motifs in their subunits and blocked the adhesion of the alpha4beta1 integrin to vascular cell adhesion molecule 1 with high selectivity. On the other hand, disintegrin EMS11 inhibited both alpha5beta1 and alpha4beta1 integrins with almost the same degree of specificity. Comparison of the amino acid sequences of the dimeric disintegrins with those of other disintegrins by multiple-sequence alignment and phylogenetic analysis, in conjunction with current biochemical and genetic data, supports the view that the different disintegrin subfamilies evolved from a common ADAM (a disintegrin and metalloproteinase-like) scaffold and that structural diversification occurred through disulphide bond engineering. This work was financed by the Dirección General de Enseñanza Superior e Investigación Científica (Madrid, Spain) (grant no. BMC2001-3337; to J. J. C.) and the American Heart Association (Dallas, TX, U.S.A.; to C. M.). Peer reviewed |
| URI: | http://dspace.mediu.edu.my:8181/xmlui/handle/10261/3631 |
| Other Identifiers: | Biochem J. 2003 June 15; 372(Pt 3): 725–734 http://dx.doi.org/10.1042/BJ20021739 0264-6021 http://hdl.handle.net/10261/3631 10.1042/BJ20021739. |
| Appears in Collections: | Digital Csic |
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