1ifq
From Proteopedia
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| - | [[Image:1ifq.jpg|left|200px]] | + | [[Image:1ifq.jpg|left|200px]] |
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| - | '''Sec22b N-terminal domain''' | + | {{Structure |
| + | |PDB= 1ifq |SIZE=350|CAPTION= <scene name='initialview01'>1ifq</scene>, resolution 2.40Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''Sec22b N-terminal domain''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1IFQ is a [ | + | 1IFQ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IFQ OCA]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11309394 11309394] |
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: five-stranded anti-parallel beta sheet]] | [[Category: five-stranded anti-parallel beta sheet]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:49:49 2008'' |
Revision as of 09:49, 20 March 2008
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| , resolution 2.40Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
Sec22b N-terminal domain
Overview
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 Structure
1IFQ is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
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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