1gl2: Difference between revisions
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<StructureSection load='1gl2' size='340' side='right' caption='[[1gl2]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='1gl2' size='340' side='right' caption='[[1gl2]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1gl2]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1gl2]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat] and [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GL2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GL2 FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gl2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gl2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1gl2 RCSB], [http://www.ebi.ac.uk/pdbsum/1gl2 PDBsum]</span></td></tr> | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gl2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gl2 OCA], [http://pdbe.org/1gl2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1gl2 RCSB], [http://www.ebi.ac.uk/pdbsum/1gl2 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 1gl2" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Buffalo rat]] | ||
[[Category: | [[Category: Lk3 transgenic mice]] | ||
[[Category: Antonin, W]] | [[Category: Antonin, W]] | ||
[[Category: Becker, S]] | [[Category: Becker, S]] | ||
Revision as of 14:19, 10 September 2015
CRYSTAL STRUCTURE OF AN ENDOSOMAL SNARE CORE COMPLEXCRYSTAL STRUCTURE OF AN ENDOSOMAL SNARE CORE COMPLEX
Structural highlights
Function[VTI1B_MOUSE] V-SNARE that mediates vesicle transport pathways through interactions with t-SNAREs on the target membrane. These interactions are proposed to mediate aspects of the specificity of vesicle trafficking and to promote fusion of the lipid bilayers. [STX7_MOUSE] May be involved in protein trafficking from the plasma membrane to the early endosome (EE) as well as in homotypic fusion of endocytic organelles. Mediates the endocytic trafficking from early endosomes to late endosomes and lysosomes (By similarity). [STX8_RAT] Vesicle trafficking protein that functions in the early secretory pathway, possibly by mediating retrograde transport from cis-Golgi membranes to the ER. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedSNARE proteins are crucial for intracellular membrane fusion in all eukaryotes. These proteins assemble into tight complexes that connect membranes and may induce fusion. The crystal structure of the neuronal core complex is represented by an unusually long bundle of four alpha-helices connected by 16 layers of mostly hydrophobic amino acids. Here we report the 1.9 A resolution crystal structure of an endosomal SNARE core complex containing four SNAREs: syntaxin 7, syntaxin 8, vti1b and endobrevin/VAMP-8. Despite limited sequence homology, the helix alignment and the layer structure of the endosomal complex are remarkably similar to those of the neuronal complex. However, subtle variations are evident that characterize different SNARE subfamilies. We conclude that the structure of the SNARE core complex is an evolutionarily conserved hallmark of all SNARE complexes and is intimately associated with the general role of SNAREs in membrane fusion. Crystal structure of the endosomal SNARE complex reveals common structural principles of all SNAREs.,Antonin W, Fasshauer D, Becker S, Jahn R, Schneider TR Nat Struct Biol. 2002 Feb;9(2):107-11. PMID:11786915[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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