The binding interface between an E2 (UBC9) and a ubiquitin homologue (UBL1)

Qin Liu, Changwen Jin, Xiubei Liao, Zhiyuan Shen, David J. Chen, Yuan Chen

Research output: Contribution to journalArticle

86 Citations (Scopus)

Abstract

Human UBC9 is a member of the E2 (ubiquitin conjugation enzyme) family of proteins. Instead of conjugating to ubiquitin, it conjugates with a ubiquitin homologue UBL1 (also known as SUMO-1, GMP1, SMTP3, PIC1, and sentrin). UBC9 has been shown to be involved in cell cycle regulation, DNA repair, and p53-dependent processes. The binding interfaces of the UBC9 and UBL1 complex have been determined by chemical shift perturbation using nuclear magnetic resonance spectroscopy. The binding site of UBL1 resides on the ubiquitin domain, and the binding site of UBC9 is located on a structurally conserved region of E2. Because the UBC9-UBL1 system shares many similarities with the ubiquitin system in structures and in conjugation with each other and with target proteins, the observed binding interfaces may be conserved in E2-ubiquitin interactions in general.

Original languageEnglish (US)
Pages (from-to)16979-16987
Number of pages9
JournalJournal of Biological Chemistry
Volume274
Issue number24
DOIs
StatePublished - Jun 11 1999
Externally publishedYes

Fingerprint

Ubiquitin
SUMO-1 Protein
Binding Sites
Chemical shift
Protein Binding
DNA Repair
Nuclear magnetic resonance spectroscopy
Cell Cycle
Proteins
Repair
Magnetic Resonance Spectroscopy
Cells
DNA
Enzymes

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Biochemistry
  • Cell Biology

Cite this

Liu, Qin ; Jin, Changwen ; Liao, Xiubei ; Shen, Zhiyuan ; Chen, David J. ; Chen, Yuan. / The binding interface between an E2 (UBC9) and a ubiquitin homologue (UBL1). In: Journal of Biological Chemistry. 1999 ; Vol. 274, No. 24. pp. 16979-16987.
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The binding interface between an E2 (UBC9) and a ubiquitin homologue (UBL1). / Liu, Qin; Jin, Changwen; Liao, Xiubei; Shen, Zhiyuan; Chen, David J.; Chen, Yuan.

In: Journal of Biological Chemistry, Vol. 274, No. 24, 11.06.1999, p. 16979-16987.

Research output: Contribution to journalArticle

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