2x3v: Difference between revisions
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< | ==Structure of The F-BAR Domain of Mouse Syndapin I== | ||
<StructureSection load='2x3v' size='340' side='right'caption='[[2x3v]], [[Resolution|resolution]] 2.45Å' scene=''> | |||
You may | == Structural highlights == | ||
or | <table><tr><td colspan='2'>[[2x3v]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X3V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2X3V FirstGlance]. <br> | ||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.45Å</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=2x3v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x3v OCA], [https://pdbe.org/2x3v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2x3v RCSB], [https://www.ebi.ac.uk/pdbsum/2x3v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2x3v ProSAT]</span></td></tr> | ||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/PACN1_MOUSE PACN1_MOUSE] May play a role in endocytosis.<ref>PMID:11082044</ref> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/x3/2x3v_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</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=2x3v ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Members of the Bin/amphiphysin/Rvs (BAR) domain protein superfamily are involved in membrane remodeling in various cellular pathways ranging from endocytic vesicle and T-tubule formation to cell migration and neuromorphogenesis. Membrane curvature induction and stabilization are encoded within the BAR or Fer-CIP4 homology-BAR (F-BAR) domains, alpha-helical coiled coils that dimerize into membrane-binding modules. BAR/F-BAR domain proteins often contain an SH3 domain, which recruits binding partners such as the oligomeric membrane-fissioning GTPase dynamin. How precisely BAR/F-BAR domain-mediated membrane deformation is regulated at the cellular level is unknown. Here we present the crystal structures of full-length syndapin 1 and its F-BAR domain. Our data show that syndapin 1 F-BAR-mediated membrane deformation is subject to autoinhibition by its SH3 domain. Release from the clamped conformation is driven by association of syndapin 1 SH3 with the proline-rich domain of dynamin 1, thereby unlocking its potent membrane-bending activity. We hypothesize that this mechanism might be commonly used to regulate BAR/F-BAR domain-induced membrane deformation and to potentially couple this process to dynamin-mediated fission. Our data thus suggest a structure-based model for SH3-mediated regulation of BAR/F-BAR domain function. | |||
Molecular basis for SH3 domain regulation of F-BAR-mediated membrane deformation.,Rao Y, Ma Q, Vahedi-Faridi A, Sundborger A, Pechstein A, Puchkov D, Luo L, Shupliakov O, Saenger W, Haucke V Proc Natl Acad Sci U S A. 2010 Apr 19. PMID:20404169<ref>PMID:20404169</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2x3v" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | [[Category: Large Structures]] | ||
== | |||
< | |||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Haucke | [[Category: Haucke V]] | ||
[[Category: Ma | [[Category: Ma Q]] | ||
[[Category: Rao | [[Category: Rao Y]] | ||
[[Category: Saenger | [[Category: Saenger W]] | ||
[[Category: Vahedi-Faridi | [[Category: Vahedi-Faridi A]] | ||
Latest revision as of 10:20, 9 May 2024
Structure of The F-BAR Domain of Mouse Syndapin I
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