Ring domains functioning as e3 ligases reveal distinct structural features: A molecular dynamics simulation study

Jian Hua Zhao, Ching Tao Yang, Josephine W. Wu, Wei Bor Tsai, Hsin Yi Lin, Hsu Wei Fang, Yih Ho, Hsuan Liang Liu

研究成果: 雜誌貢獻文章同行評審

21 引文 斯高帕斯(Scopus)

摘要

RING domain, a cysteine-rich motif that chelates two zinc ions, has been shown to regulate many biological processes such as mediating a crucial step in the ubiquitinylation pathway. In order to investigate the distinct structural features for the RING domains functioning as E3 ligases, several molecular dynamics simulations involving the c-Cbl, CNOT4 (with E3 ligase function), and p44 (no E3 ligase function) RING domains were conducted in this study. Our results reveal that the structural stability of the recognition site is a basic requirement for the RING domains functioning as E3 ligases. The structural stability of the recognition site is maintained by the hydrophobic core and hydrogen bonding network. Another important structural feature of the RING domains functioning as E3 ligases is the stable distances between the recognition site and the zinc ion binding sites S1 and S2. Moreover, the RING domains functioning as E3 ligases seem to exhibit lower β stability due to the higher proportion of proline residues in their sequences. However, no significant difference of the other secondary (α and turn) and the tertiary structural stabilities can be observed among these three RING domains.
原文英語
頁(從 - 到)65-73
頁數9
期刊Journal of Biomolecular Structure and Dynamics
26
發行號1
DOIs
出版狀態已發佈 - 八月 2008

ASJC Scopus subject areas

  • 結構生物學
  • 分子生物學

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