Chem. J. Chinese Universities ›› 2009, Vol. 30 ›› Issue (8): 1641.

• Articles • Previous Articles     Next Articles

Molecular Simulations Study on the Residue 13 in Exendin-4

WANG Song, ZHAO Xi, ZHENG Qing-Chuan*, HUANG Xu-Ri, SUN Chia-Chung   

  1. State Key Laboratory of Theoretical and Computational Chemistry, Institute of Theoretical Chemistry, Jilin University, Changchun 130023, China
  • Received:2008-12-31 Online:2009-08-10 Published:2009-08-10
  • Contact: ZHENG Qing-Chuan. E-mail: zhengqch@jlu.edu.cn
  • Supported by:

    国家自然科学基金(批准号: 20773048)、教育部博士点专项基金(批准号: 20070183046)、吉林大学基本科研业务费资助项目(批准号: 200810018)和吉林大学科研启动基金(批准号: 419080105439)资助.

Abstract:

Exendin-4 as a peptide of 39 amino acid residues is an important agonist for native GLP-1 receptor and its 13th residue is crucial for biological activity according to the mutational experiments(Tyr13→Gln13). In the present work, the role of the 13th residue in enhancing activity was investigated by means of the mole-cular dynamics simulations, molecular docking and electrostatic calculation. The results suggest that the mutated Exendin-4(Tyr13→Gln13) can strength the interactions with the receptor by adjusting itself local flexibi-lity, further increase the biological activity for GLP-1 receptor.

Key words: Exendin-4; Molecular dynamics simulation; Complex; Electrostatic interaction

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