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Comparative modeling of human NSF reveals a possible binding mode of GABARAP and GATE‐16
Author(s) -
Thielmann Yvonne,
Weiergräber Oliver H.,
Ma Peixiang,
Schwarten Melanie,
Mohrlüder Jeannine,
Willbold Dieter
Publication year - 2009
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.22477
Subject(s) - random hexamer , ubiquitin , microbiology and biotechnology , chemistry , computational biology , biophysics , biology , biochemistry , gene
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. © 2009 Wiley‐Liss, Inc.