2v0o

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{{Seed}}
 
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[[Image:2v0o.png|left|200px]]
 
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==FCHO2 F-BAR domain==
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The line below this paragraph, containing "STRUCTURE_2v0o", creates the "Structure Box" on the page.
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<StructureSection load='2v0o' size='340' side='right'caption='[[2v0o]], [[Resolution|resolution]] 2.30&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'>[[2v0o]] is a 3 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=2V0O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2V0O FirstGlance]. <br>
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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]] 2.3&#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=ACT:ACETATE+ION'>ACT</scene></td></tr>
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{{STRUCTURE_2v0o| PDB=2v0o | 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=2v0o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v0o OCA], [https://pdbe.org/2v0o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2v0o RCSB], [https://www.ebi.ac.uk/pdbsum/2v0o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2v0o ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/FCHO2_HUMAN FCHO2_HUMAN] Functions in an early step of clathrin-mediated endocytosis. Has both a membrane binding/bending activity and the ability to recruit proteins essential to the formation of functional clathrin-coated pits. Has a lipid-binding activity with a preference for membranes enriched in phosphatidylserine and phosphoinositides (Pi(4,5) biphosphate) like the plasma membrane. Its membrane-bending activity might be important for the subsequent action of clathrin and adaptors in the formation of clathrin-coated vesicles. Involved in adaptor protein complex AP-2-dependent endocytosis of the transferrin receptor, it also functions in the AP-2-independent endocytosis of the LDL receptor.<ref>PMID:17540576</ref> <ref>PMID:20448150</ref> <ref>PMID:21762413</ref> <ref>PMID:22323290</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/v0/2v0o_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=2v0o 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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A spectrum of membrane curvatures exists within cells, and proteins have evolved different modules to detect, create, and maintain these curvatures. Here we present the crystal structure of one such module found within human FCHo2. This F-BAR (extended FCH) module consists of two F-BAR domains, forming an intrinsically curved all-helical antiparallel dimer with a Kd of 2.5 microM. The module binds liposomes via a concave face, deforming them into tubules with variable diameters of up to 130 nm. Pulse EPR studies showed the membrane-bound dimer is the same as the crystal dimer, although the N-terminal helix changed conformation on membrane binding. Mutation of a phenylalanine on this helix partially attenuated narrow tubule formation, and resulted in a gain of curvature sensitivity. This structure shows a distant relationship to curvature-sensing BAR modules, and suggests how similar coiled-coil architectures in the BAR superfamily have evolved to expand the repertoire of membrane-sculpting possibilities.
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===FCHO2 F-BAR DOMAIN===
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Structure and analysis of FCHo2 F-BAR domain: a dimerizing and membrane recruitment module that effects membrane curvature.,Henne WM, Kent HM, Ford MG, Hegde BG, Daumke O, Butler PJ, Mittal R, Langen R, Evans PR, McMahon HT Structure. 2007 Jul;15(7):839-52. Epub 2007 Jun 1. PMID:17540576<ref>PMID:17540576</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_17540576}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2v0o" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 17540576 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_17540576}}
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__TOC__
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</StructureSection>
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==About this Structure==
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2V0O is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V0O OCA].
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==Reference==
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Structure and analysis of FCHo2 F-BAR domain: a dimerizing and membrane recruitment module that effects membrane curvature., Henne WM, Kent HM, Ford MG, Hegde BG, Daumke O, Butler PJ, Mittal R, Langen R, Evans PR, McMahon HT, Structure. 2007 Jul;15(7):839-52. Epub 2007 Jun 1. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17540576 17540576]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Evans, P R.]]
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[[Category: Evans PR]]
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[[Category: Henne, W M.]]
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[[Category: Henne WM]]
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[[Category: Kent, H M.]]
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[[Category: Kent HM]]
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[[Category: Mcmahon, H T.]]
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[[Category: McMahon HT]]
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[[Category: Coiled-coil]]
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[[Category: Efc domain]]
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[[Category: Endocytosis]]
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[[Category: Exocytosis]]
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[[Category: F-bar domain]]
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[[Category: Lipid-binding protein]]
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[[Category: Membrane curvature]]
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[[Category: Polymorphism]]
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[[Category: Vesicle trafficking]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 08:24:08 2008''
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Current revision

FCHO2 F-BAR domain

PDB ID 2v0o

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