A closer look of the HECTic ubiquitin ligases.

Structure (London, England : 1993) ·Vol. 11 ·No. 1 ·2003-01-00 ·Pages 5-6

Zheng N

Abstract

In comparison with previous studies, a new crystal structure of a HECT ubiquitin ligase catalytic domain has revealed the structural basis of the conformational flexibility of the enzyme and provides insights into the mechanism underlying the ubiquitin transfer reaction in the polyubiquitination pathway.

MeSH Terms

Binding Sites Catalytic Domain Protein Conformation Ubiquitin/chemistry,metabolism Ubiquitin-Protein Ligases/chemistry,metabolism

Chemicals

Ubiquitin Ubiquitin-Protein Ligases

Authors & Affiliations

1 authors, click to expand affiliations / ORCID

Zheng Ning

Article Info

Journal

Structure (London, England : 1993)

Abbr.

Structure

ISSN

0969-2126

DOI

10.1016/s0969-2126(02)00940-1

Published

2003-01-00

Pages

5-6

Language

English

Region

United States

NLM ID

101087697

Subset

External Links

PubMed source DOI: 10.1016/s0969-2126(02)00940-1 View journal details

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A closer look of the HECTic ubiquitin ligases.

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