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    Nat Cell Biol. 1999 Jul;1(3):175-82.

    Crystal structure of the amino-terminal domain of N-ethylmaleimide-sensitive fusion protein.

    May AP, Misura KM, Whiteheart SW, Weis WI.

    Department of Structural Biology, Stanford University School of Medicine, California 94305, USA.

    The cytosolic ATPase N-ethylmaleimide-sensitive fusion protein (NSF) disassembles complexes of membrane-bound proteins known as SNAREs, an activity essential for vesicular trafficking. The amino-terminal domain of NSF (NSF-N) is required for the interaction of NSF with the SNARE complex through the adaptor protein alpha-SNAP. The crystal structure of NSF-N reveals two subdomains linked by a single stretch of polypeptide. A polar interface between the two subdomains indicates that they can move with respect to one another during the catalytic cycle of NSF. Structure-based sequence alignments indicate that in addition to NSF orthologues, the p97 family of ATPases contain an amino-terminal domain of similar structure.

    PMID: 10559905 [PubMed - indexed for MEDLINE]

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