Comparative modeling of human NSF reveals a possible binding mode of GABARAP and GATE‐16
doi: 10.1002/prot.22477
pmid: 19533740
Comparative modeling of human NSF reveals a possible binding mode of GABARAP and GATE‐16
AbstractVesicular 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.
- University of Duesseldorf Germany
- Heinrich Heine University Düsseldorf Germany
- Forschungszentrum Jülich Germany
Models, Molecular, Binding Sites, Protein Conformation, Ubiquitin, Hydrolysis, Microfilament Proteins, Autophagy-Related Protein 8 Family, Protein Structure, Tertiary, Adenosine Triphosphate, Protein Interaction Mapping, Humans, Phosphorylation, Apoptosis Regulatory Proteins, Peptides, Microtubule-Associated Proteins, N-Ethylmaleimide-Sensitive Proteins, Adaptor Proteins, Signal Transducing, Protein Binding
Models, Molecular, Binding Sites, Protein Conformation, Ubiquitin, Hydrolysis, Microfilament Proteins, Autophagy-Related Protein 8 Family, Protein Structure, Tertiary, Adenosine Triphosphate, Protein Interaction Mapping, Humans, Phosphorylation, Apoptosis Regulatory Proteins, Peptides, Microtubule-Associated Proteins, N-Ethylmaleimide-Sensitive Proteins, Adaptor Proteins, Signal Transducing, Protein Binding
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