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| | <StructureSection load='2d4c' size='340' side='right'caption='[[2d4c]], [[Resolution|resolution]] 2.40Å' scene=''> | | <StructureSection load='2d4c' size='340' side='right'caption='[[2d4c]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2d4c]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D4C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2D4C FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2d4c]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D4C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2D4C FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</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]] 2.4Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1x03|1x03]], [[1x04|1x04]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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=2d4c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d4c OCA], [http://pdbe.org/2d4c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2d4c RCSB], [http://www.ebi.ac.uk/pdbsum/2d4c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2d4c 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=2d4c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d4c OCA], [https://pdbe.org/2d4c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2d4c RCSB], [https://www.ebi.ac.uk/pdbsum/2d4c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2d4c ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SH3G2_HUMAN SH3G2_HUMAN]] Implicated in synaptic vesicle endocytosis. May recruit other proteins to membranes with high curvature. | + | [https://www.uniprot.org/uniprot/SH3G2_HUMAN SH3G2_HUMAN] Implicated in synaptic vesicle endocytosis. May recruit other proteins to membranes with high curvature. |
| | == 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: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Masuda, M]] | + | [[Category: Masuda M]] |
| - | [[Category: Takeda, S]] | + | [[Category: Takeda S]] |
| - | [[Category: Bar domain]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
SH3G2_HUMAN Implicated in synaptic vesicle endocytosis. May recruit other proteins to membranes with high curvature.
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
The crescent-shaped BAR (Bin/Amphiphysin/Rvs-homology) domain dimer is a versatile protein module that senses and generates positive membrane curvature. The BAR domain dimer of human endophilin-A1, solved at 3.1 A, has a unique structure consisting of a pair of helix-loop appendages sprouting out from the crescent. The appendage's short helices form a hydrophobic ridge, which runs across the concave surface at its center. Examining liposome binding and tubulation in vitro using purified BAR domain and its mutants indicated that the ridge penetrates into the membrane bilayer and enhances liposome tubulation. BAR domain-expressing cells exhibited marked plasma membrane tubulation in vivo. Furthermore, a swinging-arm mutant lost liposome tubulation activity yet retaining liposome binding. These data suggested that the rigid crescent dimer shape is crucial for the tubulation. We here propose that the BAR domain drives membrane curvature by coordinate action of the crescent's scaffold mechanism and the ridge's membrane insertion in addition to membrane binding via amino-terminal amphipathic helix.
Endophilin BAR domain drives membrane curvature by two newly identified structure-based mechanisms.,Masuda M, Takeda S, Sone M, Ohki T, Mori H, Kamioka Y, Mochizuki N EMBO J. 2006 Jun 21;25(12):2889-97. Epub 2006 Jun 8. PMID:16763557[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Masuda M, Takeda S, Sone M, Ohki T, Mori H, Kamioka Y, Mochizuki N. Endophilin BAR domain drives membrane curvature by two newly identified structure-based mechanisms. EMBO J. 2006 Jun 21;25(12):2889-97. Epub 2006 Jun 8. PMID:16763557
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