The hexamerization domain of N-ethylmaleimide-sensitive factor: structural clues to chaperone function

Neuwald, A. F. (February 1999) The hexamerization domain of N-ethylmaleimide-sensitive factor: structural clues to chaperone function. Structure, 7 (2). R19-23. ISSN 0969-2126 (Print)

URL: http://www.ncbi.nlm.nih.gov/pubmed/10368290
DOI: 10.1016/S0969-2126(99)80015-X

Abstract

The hexameric structure of the D2 ATP-binding module of N-ethylmaleimide-sensitive factor (NSF), a chaperone involved in SNARE complex disassembly, was recently determined. This structure and the previously determined structure of the DNA polymerase III delta' subunit have far-reaching biological significance because these modules are related to diverse ATPases that promote the assembly, disassembly and operation of various protein complexes.

Item Type: Paper
Uncontrolled Keywords: Adenosine Triphosphate/metabolism Amino Acid Sequence Carrier Proteins/ chemistry Membrane Proteins/metabolism Models, Molecular Molecular Chaperones/ chemistry Molecular Sequence Data N-Ethylmaleimide-Sensitive Proteins Protein Conformation Research Support, U.S. Gov't, P.H.S. SNARE Proteins Sequence Alignment Vesicular Transport Proteins
Subjects: bioinformatics > genomics and proteomics > small molecules > ATP
bioinformatics > genomics and proteomics > design > amino acid design
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification
CSHL Authors:
Communities: CSHL labs > Neuwald lab
Depositing User: Kathleen Darby
Date: 15 February 1999
Date Deposited: 23 Apr 2014 20:46
Last Modified: 23 Apr 2014 20:46
Related URLs:
URI: http://repository.cshl.edu/id/eprint/29825

Actions (login required)

Administrator's edit/view item Administrator's edit/view item
CSHL HomeAbout CSHLResearchEducationNews & FeaturesCampus & Public EventsCareersGiving