Molecular dynamics simulations to investigate the effects of zinc ions on the structural stability of the c-Cbl RING domain

Hsuan Liang Liu, Ching Tao Yang, Jian Hua Zhao, Chih Hung Huang, Hsin Yi Lin, Hsu Wei Fang, Yih Ho, Wei Bor Tsai

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

In eukaryotic cells, ubiquitylation of proteins plays a critical role in regulating diverse cell processes by the ubiquitin activating enzyme (E1), ubiquitin-conjugating enzyme (E2), and ubiquitin protein ligase (E3). E3 is the key component that confers specificity to ubiquitylation and directs the conjugation of ubiquitin to a specific target protein. RING domains are small structured protein domains that require the coordination of zinc ions for a stable tertiary fold and some of them are involved in the E3 family. In this study, we reported the detailed relationships between the two zinc ions and the structural stability of the c-Cbl RING domain by molecular dynamics simulations. Our results show that these two zinc ions play an important role in maintaining both the secondary and tertiary structural stabilities of the c-Cbl RING domain. Our results also reveal that the secondary structural stability of the c-Cbl RING domain is mainly determined by the hydrogen-bonding networks in or near the two zinc ion binding sites. Our results further demonstrate that zinc ion binding site 2 is more structurally stable than site 1.

Original languageEnglish
Pages (from-to)1231-1238
Number of pages8
JournalBiotechnology Progress
Volume23
Issue number5
DOIs
Publication statusPublished - Sep 2007

ASJC Scopus subject areas

  • Food Science
  • Biotechnology
  • Microbiology

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