1qkr

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[[Image:1qkr.png|left|200px]]
 
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==Crystal structure of the vinculin tail and a pathway for activation==
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The line below this paragraph, containing "STRUCTURE_1qkr", creates the "Structure Box" on the page.
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<StructureSection load='1qkr' size='340' side='right'caption='[[1qkr]], [[Resolution|resolution]] 1.80&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'>[[1qkr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QKR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QKR 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]] 1.8&#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>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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{{STRUCTURE_1qkr| PDB=1qkr | 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=1qkr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qkr OCA], [https://pdbe.org/1qkr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qkr RCSB], [https://www.ebi.ac.uk/pdbsum/1qkr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qkr ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/VINC_CHICK VINC_CHICK] Actin filament (F-actin)-binding protein involved in cell-matrix adhesion and cell-cell adhesion. Regulates cell-surface E-cadherin expression and potentiates mechanosensing by the E-cadherin complex. May also play important roles in cell morphology and locomotion.<ref>PMID:15229287</ref> <ref>PMID:20584916</ref> <ref>PMID:20086044</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/qk/1qkr_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=1qkr 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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Vinculin plays a dynamic role in the assembly of the actin cytoskeleton. A strong interaction between its head and tail domains that regulates binding to other cytoskeletal components is disrupted by acidic phospholipids. Here, we present the crystal structure of the vinculin tail, residues 879-1066. Five amphipathic helices form an antiparallel bundle that resembles exchangeable apolipoproteins. A C-terminal arm wraps across the base of the bundle and emerges as a hydrophobic hairpin surrounded by a collar of basic residues, adjacent to the N terminus. We show that the C-terminal arm is required for binding to acidic phospholipids but not to actin, and that binding either ligand induces conformational changes that may represent the first step in activation.
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===CRYSTAL STRUCTURE OF THE VINCULIN TAIL AND A PATHWAY FOR ACTIVATION===
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Crystal structure of the vinculin tail suggests a pathway for activation.,Bakolitsa C, de Pereda JM, Bagshaw CR, Critchley DR, Liddington RC Cell. 1999 Dec 10;99(6):603-13. PMID:10612396<ref>PMID:10612396</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_10612396}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1qkr" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 10612396 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10612396}}
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==About this Structure==
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[[1qkr]] is a 2 chain structure of [[Vinculin]] with sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QKR OCA].
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==See Also==
==See Also==
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*[[Vinculin]]
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*[[Vinculin 3D structures|Vinculin 3D structures]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:10612396</ref><references group="xtra"/>
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__TOC__
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</StructureSection>
[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
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[[Category: Bagshaw, C R.]]
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[[Category: Large Structures]]
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[[Category: Bakolitsa, C.]]
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[[Category: Bagshaw CR]]
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[[Category: Critchley, D R.]]
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[[Category: Bakolitsa C]]
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[[Category: Liddington, R C.]]
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[[Category: Critchley DR]]
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[[Category: Pereda, J M.De.]]
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[[Category: De Pereda JM]]
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[[Category: Actin cytoskeleton]]
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[[Category: Liddington RC]]
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[[Category: Cell adhesion]]
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[[Category: Helical bundle]]
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[[Category: Lipid binding]]
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Current revision

Crystal structure of the vinculin tail and a pathway for activation

PDB ID 1qkr

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