| A conserved asparagine has a structural role in ubiquitin-conjugating enzymes. | |
| | |
MedLine Citation:
|
PMID: 23292652 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
|
It is widely accepted that ubiquitin-conjugating enzymes contain an active site asparagine that serves as an oxyanion hole, thereby stabilizing a negatively charged transition state intermediate and promoting ubiquitin transfer. Using structural and biochemical approaches to study the role of the conserved asparagine to ubiquitin conjugation by Ubc13-Mms2, we conclude that the importance of this residue stems primarily from its structural role in stabilizing an active site loop. |
| | |
Authors:
|
Christopher E Berndsen; Reuven Wiener; Ian W Yu; Alison E Ringel; Cynthia Wolberger |
Publication Detail:
|
Type: JOURNAL ARTICLE Date: 2013-1-06 |
Journal Detail:
|
Title: Nature chemical biology Volume: - ISSN: 1552-4469 ISO Abbreviation: Nat. Chem. Biol. Publication Date: 2013 Jan |
Date Detail:
|
Created Date: 2013-1-7 Completed Date: - Revised Date: - |
Medline Journal Info:
|
Nlm Unique ID: 101231976 Medline TA: Nat Chem Biol Country: - |
Other Details:
|
Languages: ENG Pagination: - Citation Subset: - |
Affiliation:
|
1] Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, Maryland, USA. [2] Howard Hughes Medical Institute, Johns Hopkins University School of Medicine, Baltimore, Maryland, USA. [3] Department of Chemistry and Biochemistry, James Madison University, Harrisonburg, Virginia, USA. |
Export Citation:
|
APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
|
|
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
Previous Document: Small-molecule activation of the TRAIL receptor DR5 in human cancer cells.
Next Document: Discovery of a chemical probe for the L3MBTL3 methyllysine reader domain.