J Biol Chem. 1999 Jun 11;274(24):16979-87.

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

Liu Q, Jin C, Liao X, Shen Z, Chen DJ, Chen Y.

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Division of Immunology, Beckman Research Institute of the City of Hope, Duarte, California 91010, USA.

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.

PMID:: 10358047; [PubMed - indexed for MEDLINE]

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

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