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)
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: | https://repository.cshl.edu/id/eprint/29825 |
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