1fq1: Difference between revisions

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-[[Image:1fq1.gif|left|200px]]<br />
-<applet load="1fq1" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1fq1, resolution 3.0&Aring;" />
-'''CRYSTAL STRUCTURE OF KINASE ASSOCIATED PHOSPHATASE (KAP) IN COMPLEX WITH PHOSPHO-CDK2'''<br />
-==Overview==
+==CRYSTAL STRUCTURE OF KINASE ASSOCIATED PHOSPHATASE (KAP) IN COMPLEX WITH PHOSPHO-CDK2==
-The CDK-interacting protein phosphatase KAP dephosphorylates, phosphoThr-160 (pThr-160) of the CDK2 activation segment, the site of, regulatory phosphorylation that is essential for kinase activity. Here we, describe the crystal structure of KAP in association with pThr-160-CDK2, representing an example of a protein phosphatase in complex with its, intact protein substrate. The major protein interface between the two, molecules is formed by the C-terminal lobe of CDK2 and the C-terminal, helix of KAP, regions remote from the kinase-activation segment and the, KAP catalytic site. The kinase-activation segment interacts with the, catalytic site of KAP almost entirely via the phosphate group of pThr-160., This interaction requires that the activation segment is unfolded and, drawn away from the kinase molecule, inducing a conformation of CDK2, similar to the activated state observed in the CDK2/cyclin A complex.
+<StructureSection load='1fq1' size='340' side='right'caption='[[1fq1]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1fq1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FQ1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FQ1 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]] 3&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene></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=1fq1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fq1 OCA], [https://pdbe.org/1fq1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fq1 RCSB], [https://www.ebi.ac.uk/pdbsum/1fq1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fq1 ProSAT]</span></td></tr>
+</table>
+== 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/fq/1fq1_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1fq1 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The CDK-interacting protein phosphatase KAP dephosphorylates phosphoThr-160 (pThr-160) of the CDK2 activation segment, the site of regulatory phosphorylation that is essential for kinase activity. Here we describe the crystal structure of KAP in association with pThr-160-CDK2, representing an example of a protein phosphatase in complex with its intact protein substrate. The major protein interface between the two molecules is formed by the C-terminal lobe of CDK2 and the C-terminal helix of KAP, regions remote from the kinase-activation segment and the KAP catalytic site. The kinase-activation segment interacts with the catalytic site of KAP almost entirely via the phosphate group of pThr-160. This interaction requires that the activation segment is unfolded and drawn away from the kinase molecule, inducing a conformation of CDK2 similar to the activated state observed in the CDK2/cyclin A complex.
-==About this Structure==
+Phosphoprotein-protein interactions revealed by the crystal structure of kinase-associated phosphatase in complex with phosphoCDK2.,Song H, Hanlon N, Brown NR, Noble ME, Johnson LN, Barford D Mol Cell. 2001 Mar;7(3):615-26. PMID:11463386<ref>PMID:11463386</ref>
-FQ1 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with MG and ATP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FQ1 OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-Phosphoprotein-protein interactions revealed by the crystal structure of kinase-associated phosphatase in complex with phosphoCDK2., Song H, Hanlon N, Brown NR, Noble ME, Johnson LN, Barford D, Mol Cell. 2001 Mar;7(3):615-26. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11463386 11463386]
+</div>
+<div class="pdbe-citations 1fq1" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Cyclin-dependent kinase 3D structures|Cyclin-dependent kinase 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Protein complex]]
+[[Category: Large Structures]]
-[[Category: Protein-tyrosine-phosphatase]]
+[[Category: Barford D]]
-[[Category: Barford, D.]]
+[[Category: Brown NR]]
-[[Category: Brown, N.R.]]
+[[Category: Hanlon N]]
-[[Category: Hanlon, N.]]
+[[Category: Johnson LN]]
-[[Category: Johnson, L.N.]]
+[[Category: Noble MEM]]
-[[Category: Noble, M.E.M.]]
+[[Category: Song H]]
-[[Category: Song, H.]]
-[[Category: ATP]]
-[[Category: MG]]
-[[Category: phospho-protein/protein complex]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:56:06 2007''