Linked Life Data

11309394

Source:http://linkedlifedata.com/resource/pubmed/id/11309394

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pubmed-article:11309394pubmed:abstractTextIntra-cellular membrane fusion is facilitated by the association of SNAREs from opposite membranes into stable alpha-helical bundles. Many SNAREs, in addition to their alpha-helical regions, contain N-terminal domains that likely have essential regulatory functions. To better understand this regulation, we have determined the 2.4-A crystal structure of the 130-amino acid N-terminal domain of mouse Sec22b (mSec22b), a SNARE involved in endoplasmic reticulum/Golgi membrane trafficking. The domain consists of a mixed alpha-helical/beta-sheet fold that resembles a circular permutation of the actin/poly-proline binding protein, profilin, and the GAF/PAS family of regulatory modules. The structure is distinct from the previously characterized N-terminal domain of syntaxin 1A, and, unlike syntaxin 1A, the N-terminal domain of mSec22b has no effect on the rate of SNARE assembly in vitro. An analysis of surface conserved residues reveals a potential protein interaction site. Key residues in this site are distinct in two mammalian Sec22 variants that lack SNARE domains. Finally, sequence analysis indicates that a similar domain is likely present in the endosomal/lysosomal SNARE VAMP7.lld:pubmed
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pubmed-article:11309394pubmed:authorpubmed-author:SchellerR HRHlld:pubmed
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pubmed-article:11309394pubmed:articleTitleA novel snare N-terminal domain revealed by the crystal structure of Sec22b.lld:pubmed
pubmed-article:11309394pubmed:affiliationDepartment of Molecular and Cellular Physiology, Howard Hughes Medical Institute and the Department of Structural Biology, Stanford University School of Medicine, Stanford, California 94305, USA.lld:pubmed
pubmed-article:11309394pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:11309394pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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