1ayr

<StructureSection load='1ayr' size='340' side='right' caption='[[1ayr]], [[Resolution|resolution]] 3.30&Aring;' scene=''>

<table><tr><td colspan='2'>[[1ayr]] is a 4 chain structure with 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=1AYR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ayr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ayr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ayr RCSB], [http://www.ebi.ac.uk/pdbsum/1ayr PDBsum]</span></td></tr>

[[http://www.uniprot.org/uniprot/ARRS_BOVIN ARRS_BOVIN]] Note=S-antigen induces autoimmune uveitis.

[[http://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.

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ay/1ayr_consurf.spt"</scriptWhenChecked>

</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/chain_selection.php?pdb_ID=2ata ConSurf].

<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.

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>

== References ==

[[Category: Bueldt, G]]

[[Category: Choe, H W]]

[[Category: Granzin, J]]

[[Category: Krafft, B]]

[[Category: Labahn, J]]

[[Category: Wilden, U]]

[[Category: Sensory transduction]]