Dynamics and functional differences between dendroaspin and rhodostomin: Insights into protein scaffolds in integrin recognition

Chun Ho Cheng, Yi Chun Chen, Jia Hau Shiu, Yao Tsung Chang, Yung Sheng Chang, Chun Hau Huang, Chiu Yueh Chen, Woei Jer Chuang

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3 Citations (Scopus)


Dendroaspin (Den) and rhodostomin (Rho) are snake venom proteins containing a PRGDMP motif. Although Den and Rho have different 3D structures, they are highly potent integrin inhibitors. To study their structure, function, and dynamics relationships, we expressed Den and Rho in Pichia pastoris. The recombinant Den and Rho inhibited platelet aggregation with the KI values of 149.8 and 83.2 nM. Cell adhesion analysis showed that Den was 3.7 times less active than Rho when inhibiting the integrin αIIbβ3 and 2.5 times less active when inhibiting the integrin αvβ3. In contrast, Den and Rho were similarly active when inhibiting the integrin α5β1 with the IC50values of 239.8 and 256.8 nM. NMR analysis showed that recombinant Den and Rho have different 3D conformations for their arginyl-glycyl-aspartic acid (RGD) motif. However, the comparison with Rho showed that the docking of Den into integrin αvβ3 resulted in a similar number of contacts. Analysis of the dynamic properties of the RGD loop in Den and Rho showed that they also had different dynamic properties. These results demonstrate that protein scaffolds affect the function, structure, and dynamics of their RGD motif. Published by Wiley-Blackwell.

Original languageEnglish
Pages (from-to)1872-1884
Number of pages13
JournalProtein Science
Issue number12
Publication statusPublished - 2012 Dec 1


All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology

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