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|   | <StructureSection load='2c08' size='340' side='right'caption='[[2c08]], [[Resolution|resolution]] 2.90Å' scene=''>  |   | <StructureSection load='2c08' size='340' side='right'caption='[[2c08]], [[Resolution|resolution]] 2.90Å' scene=''>  | 
|   | == Structural highlights ==  |   | == Structural highlights ==  | 
| - | <table><tr><td colspan='2'>[[2c08]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C08 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C08 FirstGlance]. <br>  | + | <table><tr><td colspan='2'>[[2c08]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C08 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C08 FirstGlance]. <br>  | 
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>  | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9Å</td></tr>  | 
|   | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>  | 
|   | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2c08 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c08 OCA], [https://pdbe.org/2c08 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2c08 RCSB], [https://www.ebi.ac.uk/pdbsum/2c08 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2c08 ProSAT]</span></td></tr>  |   | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2c08 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c08 OCA], [https://pdbe.org/2c08 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2c08 RCSB], [https://www.ebi.ac.uk/pdbsum/2c08 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2c08 ProSAT]</span></td></tr>  | 
|   | </table>  |   | </table>  | 
|   | + | == Function ==  | 
|   | + | [https://www.uniprot.org/uniprot/SH3G2_RAT SH3G2_RAT] Implicated in synaptic vesicle endocytosis. May recruit other proteins to membranes with high curvature.<ref>PMID:11604418</ref> <ref>PMID:16763559</ref>   | 
|   | == Evolutionary Conservation ==  |   | == Evolutionary Conservation ==  | 
|   | [[Image:Consurf_key_small.gif|200px|right]]  |   | [[Image:Consurf_key_small.gif|200px|right]]  | 
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|   | __TOC__  |   | __TOC__  | 
|   | </StructureSection>  |   | </StructureSection>  | 
| - | [[Category: Buffalo rat]]  |   | 
|   | [[Category: Large Structures]]  |   | [[Category: Large Structures]]  | 
| - | [[Category: Evans, P R]]  | + | [[Category: Rattus norvegicus]]  | 
| - | [[Category: Gallop, J L]]  | + | [[Category: Evans PR]]  | 
| - | [[Category: Kent, H M]]  | + | [[Category: Gallop JL]]  | 
| - | [[Category: Mcmahon, H T]]  | + | [[Category: Kent HM]]  | 
| - | [[Category: Acyltransferase]]  | + | [[Category: Mcmahon HT]]  | 
| - | [[Category: Bar domain]]
  | + |  | 
| - | [[Category: Coiled coil]]
  | + |  | 
| - | [[Category: Endocytosis]]
  | + |  | 
| - | [[Category: Lipid-binding]]
  | + |  | 
| - | [[Category: Membrane curvature]]
  | + |  | 
| - | [[Category: Multigene family]]
  | + |  | 
| - | [[Category: Phosphorylation]]
  | + |  | 
| - | [[Category: Sh3 domain]]
  | + |  | 
| - | [[Category: Transferase]]
  | + |  | 
 |   Structural highlights 
  Function 
SH3G2_RAT Implicated in synaptic vesicle endocytosis. May recruit other proteins to membranes with high curvature.[1] [2] 
 
  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 PubMed 
Endophilin-A1 is a BAR domain-containing protein enriched at synapses and is implicated in synaptic vesicle endocytosis. It binds to dynamin and synaptojanin via a C-terminal SH3 domain. We examine the mechanism by which the BAR domain and an N-terminal amphipathic helix, which folds upon membrane binding, work as a functional unit (the N-BAR domain) to promote dimerisation and membrane curvature generation. By electron paramagnetic resonance spectroscopy, we show that this amphipathic helix is peripherally bound in the plane of the membrane, with the midpoint of insertion aligned with the phosphate level of headgroups. This places the helix in an optimal position to effect membrane curvature generation. We solved the crystal structure of rat endophilin-A1 BAR domain and examined a distinctive insert protruding from the membrane interaction face. This insert is predicted to form an additional amphipathic helix and is important for curvature generation. Its presence defines an endophilin/nadrin subclass of BAR domains. We propose that N-BAR domains function as low-affinity dimers regulating binding partner recruitment to areas of high membrane curvature.
 Mechanism of endophilin N-BAR domain-mediated membrane curvature.,Gallop JL, Jao CC, Kent HM, Butler PJ, Evans PR, Langen R, McMahon HT EMBO J. 2006 Jun 21;25(12):2898-910. Epub 2006 Jun 8. PMID:16763559[3]
 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. 
 
 
  References 
- ↑ Farsad K, Ringstad N, Takei K, Floyd SR, Rose K, De Camilli P. Generation of high curvature membranes mediated by direct endophilin bilayer interactions. J Cell Biol. 2001 Oct 15;155(2):193-200. Epub 2001 Oct 15. PMID:11604418 doi:10.1083/jcb.200107075
 
- ↑ Gallop JL, Jao CC, Kent HM, Butler PJ, Evans PR, Langen R, McMahon HT. Mechanism of endophilin N-BAR domain-mediated membrane curvature. EMBO J. 2006 Jun 21;25(12):2898-910. Epub 2006 Jun 8. PMID:16763559
 
- ↑ Gallop JL, Jao CC, Kent HM, Butler PJ, Evans PR, Langen R, McMahon HT. Mechanism of endophilin N-BAR domain-mediated membrane curvature. EMBO J. 2006 Jun 21;25(12):2898-910. Epub 2006 Jun 8. PMID:16763559
  
 
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