2csn: Difference between revisions

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-[[Image:2csn.jpg|left|200px]]
- {{Structure
+==BINARY COMPLEX OF CASEIN KINASE-1 WITH CKI7==
-|PDB= 2csn |SIZE=350|CAPTION= <scene name='initialview01'>2csn</scene>, resolution 2.50&Aring;
+<StructureSection load='2csn' size='340' side='right'caption='[[2csn]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=CKI:N-(2-AMINOETHYL)-5-CHLOROISOQUINOLINE-8-SULFONAMIDE'>CKI</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
+<table><tr><td colspan='2'>[[2csn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Schizosaccharomyces_pombe Schizosaccharomyces pombe]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CSN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CSN FirstGlance]. <br>
-|ACTIVITY=
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
-|GENE=
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CKI:N-(2-AMINOETHYL)-5-CHLOROISOQUINOLINE-8-SULFONAMIDE'>CKI</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-|DOMAIN=
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2csn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2csn OCA], [https://pdbe.org/2csn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2csn RCSB], [https://www.ebi.ac.uk/pdbsum/2csn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2csn ProSAT]</span></td></tr>
-|RELATEDENTRY=
+</table>
-|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2csn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2csn OCA], [http://www.ebi.ac.uk/pdbsum/2csn PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2csn RCSB]</span>
+== Function ==
-}}
+[https://www.uniprot.org/uniprot/CKI1_SCHPO CKI1_SCHPO] Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates.
+== 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/cs/2csn_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=2csn ConSurf].
+<div style="clear:both"></div>
-'''BINARY COMPLEX OF CASEIN KINASE-1 WITH CKI7'''
+==See Also==
+*[[Casein kinase 3D structures|Casein kinase 3D structures]]
+__TOC__
-==Overview==
+</StructureSection>
-A large family of isoquinoline sulfonamide compounds inhibits protein kinases by competing with adenosine triphosphates(ATP), yet interferes little with the activity of other ATP-using enzymes such as ATPases and adenylate cyclases. One such compound, N-(2-aminoethyl)-5-chloroisoquinoline-8-sulfonamide (CK17), is selective for casein kinase-1 isolated from a variety of sources. Here we report the crystal structure of the catalytic domain of Schizosaccharomyces pombe casein kinase-1 complexed with CK17, refined to a crystallographic R-factor of 17.8% at 2.5 angstrom resolution. The structure provides new insights into the mechanism of the ATP-competing inhibition and the origin of their selectivity toward different protein kinases. Selectivity for protein kinases versus other enzymes is achieved by hydrophobic contacts and the hydrogen bond with isoquinoline ring. We propose that the hydrogen bond involving the ring nitrogen-2 atom of the isoquinoline must be preserved, but that the ring can flip depending on the chemical substituents at ring positions 5 and 8. Selectivity for individual members of the protein kinase family is achieved primarily by interactions with these substituents.
+[[Category: Large Structures]]
-==About this Structure==
-CSN is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Schizosaccharomyces_pombe Schizosaccharomyces pombe]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CSN OCA].
-==Reference==
-Structural basis for selectivity of the isoquinoline sulfonamide family of protein kinase inhibitors., Xu RM, Carmel G, Kuret J, Cheng X, Proc Natl Acad Sci U S A. 1996 Jun 25;93(13):6308-13. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8692811 8692811]
 [[Category: Schizosaccharomyces pombe]]
-[[Category: Single protein]]
+[[Category: Cheng X]]
-[[Category: Cheng, X.]]
+[[Category: Xu R-M]]
-[[Category: Xu, R M.]]
-[[Category: casein kinase-1]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:25:59 2008''