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1cf1

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(New page: 200px<br /><applet load="1cf1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cf1, resolution 2.8&Aring;" /> '''ARRESTIN FROM BOVINE ...)
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[[Image:1cf1.gif|left|200px]]<br /><applet load="1cf1" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1cf1, resolution 2.8&Aring;" />
 
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'''ARRESTIN FROM BOVINE ROD OUTER SEGMENTS'''<br />
 
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==Overview==
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==ARRESTIN FROM BOVINE ROD OUTER SEGMENTS==
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G protein-coupled signaling is utilized by a wide variety of eukaryotes, for communicating information from the extracellular environment. Signal, termination is achieved by the action of the arrestins, which bind to, activated, phosphorylated G protein-coupled receptors. We describe here, crystallographic studies of visual arrestin in its basal conformation. The, salient features of the structure are a bipartite molecule with an unusual, polar core. This core is stabilized in part by an extended, carboxy-terminal tail that locks the molecule into an inactive state. In, addition, arrestin is found to be a dimer of two asymmetric molecules, suggesting an intrinsic conformational plasticity. In conjunction with, biochemical and mutagenesis data, we propose a molecular mechanism by, which arrestin is activated for receptor binding.
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<StructureSection load='1cf1' size='340' side='right'caption='[[1cf1]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1cf1]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CF1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CF1 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]] 2.8&#8491;</td></tr>
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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=1cf1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cf1 OCA], [https://pdbe.org/1cf1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cf1 RCSB], [https://www.ebi.ac.uk/pdbsum/1cf1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cf1 ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/ARRS_BOVIN ARRS_BOVIN] Note=S-antigen induces autoimmune uveitis.
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== Function ==
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[https://www.uniprot.org/uniprot/ARRS_BOVIN ARRS_BOVIN] Arrestin is one of the major proteins of the ros (retinal rod outer segments); it binds to photoactivated-phosphorylated rhodopsin, thereby apparently preventing the transducin-mediated activation of phosphodiesterase. Isoform B plays a role in the phototransduction cascade.
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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/cf/1cf1_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1cf1 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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G protein-coupled signaling is utilized by a wide variety of eukaryotes for communicating information from the extracellular environment. Signal termination is achieved by the action of the arrestins, which bind to activated, phosphorylated G protein-coupled receptors. We describe here crystallographic studies of visual arrestin in its basal conformation. The salient features of the structure are a bipartite molecule with an unusual polar core. This core is stabilized in part by an extended carboxy-terminal tail that locks the molecule into an inactive state. In addition, arrestin is found to be a dimer of two asymmetric molecules, suggesting an intrinsic conformational plasticity. In conjunction with biochemical and mutagenesis data, we propose a molecular mechanism by which arrestin is activated for receptor binding.
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==About this Structure==
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The 2.8 A crystal structure of visual arrestin: a model for arrestin's regulation.,Hirsch JA, Schubert C, Gurevich VV, Sigler PB Cell. 1999 Apr 16;97(2):257-69. PMID:10219246<ref>PMID:10219246</ref>
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1CF1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CF1 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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The 2.8 A crystal structure of visual arrestin: a model for arrestin's regulation., Hirsch JA, Schubert C, Gurevich VV, Sigler PB, Cell. 1999 Apr 16;97(2):257-69. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10219246 10219246]
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</div>
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[[Category: Bos taurus]]
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<div class="pdbe-citations 1cf1" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Gurevich, V.V.]]
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[[Category: Hirsch, J.A.]]
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[[Category: Schubert, C.]]
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[[Category: Sigler, P.B.]]
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[[Category: binding to acticated and phosphorylated rhodopsin]]
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[[Category: desensitisation of the visual transduction cascade]]
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[[Category: visual arrestin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:24:21 2007''
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==See Also==
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*[[Arrestin 3D structures|Arrestin 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Bos taurus]]
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[[Category: Large Structures]]
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[[Category: Gurevich VV]]
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[[Category: Hirsch JA]]
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[[Category: Schubert C]]
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[[Category: Sigler PB]]

Current revision

ARRESTIN FROM BOVINE ROD OUTER SEGMENTS

PDB ID 1cf1

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