1ifq
Sec22b N-terminal domain
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OverviewOverview
Intra-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.
About this StructureAbout this Structure
1IFQ is a Single protein structure of sequence from Mus musculus with GOL as ligand. Full crystallographic information is available from OCA.
ReferenceReference
A novel snare N-terminal domain revealed by the crystal structure of Sec22b., Gonzalez LC Jr, Weis WI, Scheller RH, J Biol Chem. 2001 Jun 29;276(26):24203-11. Epub 2001 Apr 17. PMID:11309394
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