1ayr
From Proteopedia
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==ARRESTIN FROM BOVINE ROD OUTER SEGMENTS== | ==ARRESTIN FROM BOVINE ROD OUTER SEGMENTS== | ||
| - | <StructureSection load='1ayr' size='340' side='right' caption='[[1ayr]], [[Resolution|resolution]] 3.30Å' scene=''> | + | <StructureSection load='1ayr' size='340' side='right'caption='[[1ayr]], [[Resolution|resolution]] 3.30Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1ayr]] is a 4 chain structure with sequence from [ | + | <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> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.3Å</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> | ||
</table> | </table> | ||
== Disease == | == Disease == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/ARRS_BOVIN ARRS_BOVIN] Note=S-antigen induces autoimmune uveitis. |
== Function == | == 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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ay/1ayr_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ay/1ayr_consurf.spt"</scriptWhenChecked> |
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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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> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | 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. | ||
| - | + | ==See Also== | |
| - | + | *[[Arrestin 3D structures|Arrestin 3D structures]] | |
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
| - | [[Category: Bueldt | + | [[Category: Large Structures]] |
| - | [[Category: Choe | + | [[Category: Bueldt G]] |
| - | [[Category: Granzin | + | [[Category: Choe H-W]] |
| - | [[Category: Krafft | + | [[Category: Granzin J]] |
| - | [[Category: Labahn | + | [[Category: Krafft B]] |
| - | [[Category: Wilden | + | [[Category: Labahn J]] |
| - | + | [[Category: Wilden U]] | |
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Current revision
ARRESTIN FROM BOVINE ROD OUTER SEGMENTS
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Categories: Bos taurus | Large Structures | Bueldt G | Choe H-W | Granzin J | Krafft B | Labahn J | Wilden U
