1ayr

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Current revision (06:34, 7 February 2024) (edit) (undo)
 
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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1ayr]] 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=1AYR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AYR FirstGlance]. <br>
<table><tr><td colspan='2'>[[1ayr]] 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=1AYR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AYR FirstGlance]. <br>
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</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=1ayr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ayr OCA], [https://pdbe.org/1ayr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ayr RCSB], [https://www.ebi.ac.uk/pdbsum/1ayr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ayr ProSAT]</span></td></tr>
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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]] 3.3&#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=1ayr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ayr OCA], [https://pdbe.org/1ayr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ayr RCSB], [https://www.ebi.ac.uk/pdbsum/1ayr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ayr ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
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[[https://www.uniprot.org/uniprot/ARRS_BOVIN ARRS_BOVIN]] Note=S-antigen induces autoimmune uveitis.
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[https://www.uniprot.org/uniprot/ARRS_BOVIN ARRS_BOVIN] Note=S-antigen induces autoimmune uveitis.
== Function ==
== 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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[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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=1ayr ConSurf].
</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=1ayr ConSurf].
<div style="clear:both"></div>
<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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Retinal arrestin is the essential protein for the termination of the light response in vertebrate rod outer segments. It plays an important role in quenching the light-induced enzyme cascade by its ability to bind to phosphorylated light-activated rhodopsin (P-Rh*). Arrestins are found in various G-protein-coupled amplification cascades. Here we report on the three-dimensional structure of bovine arrestin (relative molecular mass, 45,300) at 3.3 A resolution. The crystal structure comprises two domains of antiparallel beta-sheets connected through a hinge region and one short alpha-helix on the back of the amino-terminal fold. The binding region for phosphorylated light-activated rhodopsin is located at the N-terminal domain, as indicated by the docking of the photoreceptor to the three-dimensional structure of arrestin. This agrees with the interpretation of binding studies on partially digested and mutated arrestin.
 
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X-ray crystal structure of arrestin from bovine rod outer segments.,Granzin J, Wilden U, Choe HW, Labahn J, Krafft B, Buldt G Nature. 1998 Feb 26;391(6670):918-21. PMID:9495348<ref>PMID:9495348</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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<div class="pdbe-citations 1ayr" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
*[[Arrestin 3D structures|Arrestin 3D structures]]
*[[Arrestin 3D structures|Arrestin 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Bueldt, G]]
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[[Category: Bueldt G]]
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[[Category: Choe, H W]]
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[[Category: Choe H-W]]
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[[Category: Granzin, J]]
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[[Category: Granzin J]]
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[[Category: Krafft, B]]
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[[Category: Krafft B]]
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[[Category: Labahn, J]]
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[[Category: Labahn J]]
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[[Category: Wilden, U]]
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[[Category: Wilden U]]
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[[Category: Arrestin]]
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[[Category: Rhodopsin]]
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[[Category: Sensory transduction]]
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Current revision

ARRESTIN FROM BOVINE ROD OUTER SEGMENTS

PDB ID 1ayr

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