2c08

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{{Seed}}
 
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[[Image:2c08.png|left|200px]]
 
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==Rat endophilin A1 BAR domain==
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The line below this paragraph, containing "STRUCTURE_2c08", creates the "Structure Box" on the page.
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<StructureSection load='2c08' size='340' side='right'caption='[[2c08]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<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>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9&#8491;</td></tr>
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<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>
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{{STRUCTURE_2c08| PDB=2c08 | SCENE= }}
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<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>
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c0/2c08_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2c08 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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===RAT ENDOPHILIN A1 BAR DOMAIN===
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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<ref>PMID:16763559</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_16763559}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2c08" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 16763559 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_16763559}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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2C08 is a [[Single protein]] structure of sequence from [http://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].
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/16763559 16763559]
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[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Single protein]]
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[[Category: Evans PR]]
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[[Category: Evans, P R.]]
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[[Category: Gallop JL]]
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[[Category: Gallop, J L.]]
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[[Category: Kent HM]]
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[[Category: Kent, H M.]]
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[[Category: Mcmahon HT]]
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[[Category: Mcmahon, H T.]]
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[[Category: Acyltransferase]]
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[[Category: Bar domain]]
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[[Category: Coiled coil]]
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[[Category: Endocytosis]]
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[[Category: Lipid-binding]]
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[[Category: Membrane curvature]]
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[[Category: Multigene family]]
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[[Category: Phosphorylation]]
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[[Category: Sh3 domain]]
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[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 19:54:58 2008''
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Current revision

Rat endophilin A1 BAR domain

PDB ID 2c08

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