8fut

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Current revision (06:29, 24 July 2024) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 8fut is ON HOLD until Paper Publication
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==Crystal structure of Xenopus laevis arrestin 1 - P3121 crystal form==
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<StructureSection load='8fut' size='340' side='right'caption='[[8fut]], [[Resolution|resolution]] 2.54&Aring;' scene=''>
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Authors:
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== Structural highlights ==
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<table><tr><td colspan='2'>[[8fut]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8FUT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8FUT FirstGlance]. <br>
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Description:
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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]] 2.54&#8491;</td></tr>
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[[Category: Unreleased Structures]]
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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=8fut FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8fut OCA], [https://pdbe.org/8fut PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8fut RCSB], [https://www.ebi.ac.uk/pdbsum/8fut PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8fut ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ARRS_XENLA ARRS_XENLA] Binds to photoactivated, phosphorylated RHO and terminates RHO signaling via G-proteins by competing with G-proteins for the same binding site on RHO. May play a role in preventing light-dependent degeneration of retinal photoreceptor cells.[UniProtKB:P20443]
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Xenopus laevis]]
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[[Category: Barnes CL]]
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[[Category: Calvert PD]]
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[[Category: Kiser PD]]
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[[Category: Salom D]]

Current revision

Crystal structure of Xenopus laevis arrestin 1 - P3121 crystal form

PDB ID 8fut

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