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

Research output: Contribution to journalArticle

20 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)65-73
Number of pages9
JournalJournal of Biomolecular Structure and Dynamics
Volume26
Issue number1
Publication statusPublished - Aug 2008

Keywords

  • c-Cbl
  • CNOT4
  • Molecular dynamics simulations
  • p44
  • Proteasome
  • Recognition site
  • RING domain
  • Ubiquitinylation

ASJC Scopus subject areas

  • Molecular Biology
  • Structural Biology

Fingerprint Dive into the research topics of 'RING domains functioning as E3 ligases reveal distinct structural features: A molecular dynamics simulation study'. Together they form a unique fingerprint.

  • Cite this