Chem. J. Chinese Universities ›› 2010, Vol. 31 ›› Issue (5): 1039.

• Articles • Previous Articles     Next Articles

Function of the Hydrogen-bonding Network Between the Y-S-R Motif and the Heme Propionate Groups in sGC-HNOX Domain

ZHANG Yue-Bin, CHENG Ying-Kun, LÜ Ming, ZHANG Hua-Li, LI Zheng-Qiang*   

  1. Key Laboratory for Molecular Enzymology and Engineering of the Ministry of Education, Jilin University, Changchun 130021, China
  • Received:2009-08-27 Online:2010-05-10 Published:2010-05-10
  • Contact: LI Zheng-Qiang. E-mail: lzq@jlu.edu.cn
  • Supported by:

    国家自然科学基金(批准号: 30570404, 30670458)和吉林大学研究生“985工程”创新计划项目资助.

Abstract:

Molecular dynamics methods were implemented to investigate the functions of hydrogen-bonding network between the conserved Y-S-R motif and the heme propionate groups in sGC-HNOX domain. The RMSD analysis reveals that the hydrogen-bonding network can stabilize the conformation of sGC-HNOX domain conspicuously during our simulation. The secondary structure, radius of gyration and solvent-accessible surface area of sGC-HNOX domain are not disturbed by the restraint hydrogen-bonding network. The principal component analysis on trajectory data and the heme configuration analysis indicate that the essential function of hydrogen-bonding network is to stabilize the binding of 4-E motif to 7-H motif, which is related to the structu-ral integrity of sGC-HNOX domain.

Key words: sGC-HNOX domain; Y-S-R motif; Molecular dynamics; Principal component analysis; Least-square method

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