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The hexamerization domain of N-ethylmaleimide-sensitive factor: structural clues to chaperone function
1Cold Spring Harbor Laboratory, PO Box 1001, Bungtown Road, Cold Spring Harbor, NY 11724, USA. neuwald@cshl.org
Structure (London, England : 1993)
|June 16, 1999
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.