%0 Journal Article
%A Thielmann, Y.
%A Weiergräber, O.H.
%A Ma, P.
%A Schwarten, M.
%A Mohrlüder, J.
%A Willbold, D.
%T Comparative modeling of human NSF reveals a possible binding mode of GABARAP and GATE-16
%J Proteins
%V 77
%@ 0887-3585
%C New York, NY
%I Wiley-Liss
%M PreJuSER-7510
%P 637 - 646
%D 2009
%Z Grant sponsor: Deutsche Forschungsgememschaft (DFG); Grant number: Wil472/5.
%X 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.
%K Adaptor Proteins, Signal Transducing: chemistry
%K Adenosine Triphosphate: chemistry
%K Binding Sites
%K Humans
%K Hydrolysis
%K Microfilament Proteins: chemistry
%K Microtubule-Associated Proteins: chemistry
%K Models, Molecular
%K N-Ethylmaleimide-Sensitive Proteins: chemistry
%K Peptides: chemistry
%K Phosphorylation
%K Protein Binding
%K Protein Conformation
%K Protein Interaction Mapping
%K Protein Structure, Tertiary
%K Ubiquitin: chemistry
%K Adaptor Proteins, Signal Transducing (NLM Chemicals)
%K GABARAP protein, human (NLM Chemicals)
%K GABARAPL2 protein, human (NLM Chemicals)
%K Microfilament Proteins (NLM Chemicals)
%K Microtubule-Associated Proteins (NLM Chemicals)
%K Peptides (NLM Chemicals)
%K Ubiquitin (NLM Chemicals)
%K Adenosine Triphosphate (NLM Chemicals)
%K N-Ethylmaleimide-Sensitive Proteins (NLM Chemicals)
%K J (WoSType)
%F PUB:(DE-HGF)16
%9 Journal Article
%$ pmid:19533740
%U <Go to ISI:>//WOS:000270849900013
%R 10.1002/prot.22477
%U https://juser.fz-juelich.de/record/7510