Volume 31 Issue 4 - March 3, 2017 PDF
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Effects of the RGD loop and C-terminus of rhodostomin on regulating integrin  αIIbβ3 recognition.
Yao-Tsung Chang,  Jia-Hau Shiu, Chun-Hao Huang, Yi-Chun Chen, Chiu-Yueh Chen, Yung-Sheng Chang, Woei-Jer Chuang*
Department of Biochemistry and Molecular Biology, National Cheng Kung  University College of Medicine
 
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【105 Outstanding Research Award】Special Issue

Integrins are αβ heterodimeric receptors that are expressed on virtual all cells with adhesive capacity. They are involved in many common diseases including neoplasia, tumor metastasis, immune dysfunction, ischemia-reperfusion injury, viral infections, osteoporosis, and coagulopathies. Disintegrins are a family of integrin inhibitors found in snake venoms that are potent integrin inhibitors. Our studies have shown that alternations in RGD loop and the C-terminal region of these disintegrins affect their binding specificities and affinities. Rhodostomin (Rho) is a snake venom protein isolated from Calloselasma rhodostoma. Rho is a disintegrin that inhibits platelet aggregation by blocking the binding of fibrinogen to the integrin αIIbβ3 of platelets. In our study, we have successfully expressed Rho in P. pastoris and showed that Rho possesses the same function and structure as native protein. We also used NMR spectroscopy to determine 3D structure of rhodostomin and designed a potent and selective anti-platelet agent.
3D structure of the disintegrin/integrin complex
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