期刊
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
卷 77, 期 3, 页码 637-646出版社
WILEY
DOI: 10.1002/prot.22477
关键词
N-ethylmaleimide-sensitive factor; GABARAP; comparative modeling; structure model; protein-protein interaction
资金
- Deutsche Forschungsgememschaft (DFG) [Wil472/5]
Vesicular trafficking is an important homeostatic process in eukaryotic cells which critically relies on membrane fusion. One of the essential components of the universal membrane fusion machinery is NSF (N-ethylmaleimide-sensitive factor), a large hexameric ATPase involved in disassembly of SNARE (soluble NSF attachment protein receptor) complexes. To improve our understanding of this sophisticated molecular machine, we have modeled the structure of the NSF hexamer in two alternative assemblies. Our data suggest a mechanistic concept of the operating mode of NSF which helps to explain the functional impact of post-translational modifications and mutations reported previously. Furthermore, we propose a binding site for the ubiquitin-like proteins GABARAP and GATE-16, which is supported by experimental evidence, yielding a complex with favorable surface complementarity. Proteins 2009; 77:637-646. (C) 2009 Wiley-Liss, Inc.
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