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[[Image:1cf1.gif|left|200px]]
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{{STRUCTURE_1cf1|  PDB=1cf1  |  SCENE=  }}
'''ARRESTIN FROM BOVINE ROD OUTER SEGMENTS'''


==ARRESTIN FROM BOVINE ROD OUTER SEGMENTS==
<StructureSection load='1cf1' size='340' side='right'caption='[[1cf1]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
<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>
</table>
== Disease ==
[https://www.uniprot.org/uniprot/ARRS_BOVIN ARRS_BOVIN] Note=S-antigen induces autoimmune uveitis.
== Function ==
[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.
== 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/cf/1cf1_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=1cf1 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


==Overview==
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>
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.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1CF1 is a [[Single protein]] structure of sequence from [http://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].
</div>
<div class="pdbe-citations 1cf1" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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://www.ncbi.nlm.nih.gov/pubmed/10219246 10219246]
*[[Arrestin 3D structures|Arrestin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Gurevich, V V.]]
[[Category: Gurevich VV]]
[[Category: Hirsch, J A.]]
[[Category: Hirsch JA]]
[[Category: Schubert, C.]]
[[Category: Schubert C]]
[[Category: Sigler, P B.]]
[[Category: Sigler PB]]
[[Category: Binding to acticated and phosphorylated rhodopsin]]
[[Category: Desensitisation of the visual transduction cascade]]
[[Category: Visual arrestin]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 12:39:48 2008''
Retrieved from "https://proteopedia.org/1cf1"