2rlt

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{{Seed}}
 
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[[Image:2rlt.png|left|200px]]
 
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==phosphorylated CPI-17 (22-120)==
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The line below this paragraph, containing "STRUCTURE_2rlt", creates the "Structure Box" on the page.
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<StructureSection load='2rlt' size='340' side='right'caption='[[2rlt]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2rlt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RLT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RLT FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 1 model</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene></td></tr>
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{{STRUCTURE_2rlt| PDB=2rlt | SCENE= }}
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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=2rlt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rlt OCA], [https://pdbe.org/2rlt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rlt RCSB], [https://www.ebi.ac.uk/pdbsum/2rlt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rlt ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PP14A_PIG PP14A_PIG] Inhibitor of PPP1CA. Has over 1000-fold higher inhibitory activity when phosphorylated, creating a molecular switch for regulating the phosphorylation status of PPP1CA substrates and smooth muscle contraction.<ref>PMID:9237662</ref> <ref>PMID:8720121</ref> <ref>PMID:10924361</ref> <ref>PMID:10869555</ref>
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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/rl/2rlt_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2rlt 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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Phosphorylation of endogenous inhibitor proteins for type-1 Ser/Thr phosphatase (PP1) provides a mechanism for reciprocal coordination of kinase and phosphatase activities. A myosin phosphatase inhibitor protein CPI-17 is phosphorylated at Thr38 through G-protein-mediated signals, resulting in a &gt;1000-fold increase in inhibitory potency. We show here the solution NMR structure of phospho-T38-CPI-17 with rmsd of 0.36 +/- 0.06 A for the backbone secondary structure, which reveals how phosphorylation triggers a conformational change and exposes an inhibitory surface. This active conformation is stabilized by the formation of a hydrophobic core of intercalated side chains, which is not formed in a phospho-mimetic D38 form of CPI-17. Thus, the profound increase in potency of CPI-17 arises from phosphorylation, conformational change, and hydrophobic stabilization of a rigid structure that poses the phosphorylated residue on the protein surface and restricts its hydrolysis by myosin phosphatase. Our results provide structural insights into transduction of kinase signals by PP1 inhibitor proteins.
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===phosphorylated CPI-17 (22-120)===
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Phosphorylation-induced conformational switching of CPI-17 produces a potent myosin phosphatase inhibitor.,Eto M, Kitazawa T, Matsuzawa F, Aikawa S, Kirkbride JA, Isozumi N, Nishimura Y, Brautigan DL, Ohki SY Structure. 2007 Dec;15(12):1591-602. PMID:18073109<ref>PMID:18073109</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 2rlt" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_18073109}}, adds the Publication Abstract to the page
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*[[Protein phosphatase 3D structures|Protein phosphatase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 18073109 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_18073109}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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2RLT is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RLT OCA].
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==Reference==
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<ref group="xtra">PMID:18073109</ref><references group="xtra"/>
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[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
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[[Category: Cytoplasm]]
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[[Category: Eto M]]
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[[Category: Hydrolase]]
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[[Category: Phosphorylation]]
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[[Category: Pp1 inhibitor]]
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[[Category: Protein phosphatase inhibitor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 09:17:38 2009''
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Current revision

phosphorylated CPI-17 (22-120)

PDB ID 2rlt

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