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

Authors
Neuwald, AF
Citation
Af. Neuwald, The hexamerization domain of N-ethylmaleimide-sensitive factor: structuralclues to chaperone function, STRUCT F D, 7(2), 1999, pp. R19-R23
Citations number
23
Categorie Soggetti
Biochemistry & Biophysics
Journal title
STRUCTURE WITH FOLDING & DESIGN
ISSN journal
09692126 → ACNP
Volume
7
Issue
2
Year of publication
1999
Pages
R19 - R23
Database
ISI
SICI code
0969-2126(19990215)7:2<R19:THDONF>2.0.ZU;2-0
Abstract
The hexameric structure of the D2 ATP-binding module of N-ethylmaleimide-se nsitive factor (NSF), a chaperone involved in SNARE complex disassembly, wa s recently determined. This structure and the previously determined structu re of the DNA polymerase III delta' subunit have far-reaching biological si gnificance because these modules are related to diverse ATPases that promot e the assembly, disassembly and operation of various protein complexes.