1ifq: Difference between revisions
No edit summary |
No edit summary |
||
Line 1: | Line 1: | ||
[[Image:1ifq.jpg|left|200px]] | [[Image:1ifq.jpg|left|200px]] | ||
'''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= | |||
}} | |||
'''Sec22b N-terminal domain''' | |||
==Overview== | ==Overview== | ||
Line 7: | Line 16: | ||
==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]] | ||
Line 20: | Line 29: | ||
[[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 12:49, 20 March 2008
| |||||||
, resolution 2.40Å | |||||||
---|---|---|---|---|---|---|---|
Ligands: | |||||||
Coordinates: | save as pdb, mmCIF, xml |
Sec22b N-terminal domain
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. 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
Page seeded by OCA on Thu Mar 20 11:49:49 2008