2cyh: Difference between revisions

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-[[Image:2cyh.jpg|left|200px]]
-<!--
+==CYCLOPHILIN A COMPLEXED WITH DIPEPTIDE ALA-PRO==
-The line below this paragraph, containing "STRUCTURE_2cyh", creates the "Structure Box" on the page.
+<StructureSection load='2cyh' size='340' side='right'caption='[[2cyh]], [[Resolution|resolution]] 1.64&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[2cyh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1cyh 1cyh]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CYH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CYH FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.64&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ALA:ALANINE'>ALA</scene>, <scene name='pdbligand=PRO:PROLINE'>PRO</scene></td></tr>
-{{STRUCTURE_2cyh|  PDB=2cyh  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2cyh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cyh OCA], [https://pdbe.org/2cyh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cyh RCSB], [https://www.ebi.ac.uk/pdbsum/2cyh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cyh ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/PPIA_HUMAN PPIA_HUMAN] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
+== 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/cy/2cyh_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=2cyh ConSurf].
+<div style="clear:both"></div>
-'''CYCLOPHILIN A COMPLEXED WITH DIPEPTIDE ALA-PRO'''
+==See Also==
+*[[Cyclophilin 3D structures|Cyclophilin 3D structures]]
+__TOC__
-==Overview==
+</StructureSection>
-The structures of cyclophilin A complexed with dipeptides of Ser-Pro, His-Pro, and Gly-Pro have been determined and refined at high resolution. Comparison of these structures revealed that the dipeptide complexes have the same molecular conformation and the same binding of the dipeptides. The side chains of the N-terminal amino acid of the above dipeptides do not strongly interact with cyclophilin, implying their minor contribution to the cis-trans isomerization and thus accounting for the broad catalytic specificity of the enzyme. The binding of the dipeptides is similar to that of the common substrate succinyl-Ala-Ala-Pro-Phe-p-nitroanilide in terms of the N-terminal hydrogen bonding and the hydrophobic interaction of the proline side chain. However, substantial difference between these structures are observed in (1) hydrogen bonding between the carboxyl terminus of the peptides and Arg55 and between Arg55 and Gln63, (2) the side chain conformation of Arg55, and (3) water binding at the active site. These differences imply either that dipeptides are not substrates but competitive inhibitors of peptidyl-prolyl cis-trans isomerases or that dipeptides are subject to different catalytic mechanisms from tetrapeptides.
-==About this Structure==
-CYH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1cyh 1cyh]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CYH OCA].
-==Reference==
-Mechanistic implication of crystal structures of the cyclophilin-dipeptide complexes., Zhao Y, Ke H, Biochemistry. 1996 Jun 11;35(23):7362-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8652512 8652512]
 [[Category: Homo sapiens]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Ke, H.]]
+[[Category: Ke H]]
-[[Category: Zhao, Y.]]
+[[Category: Zhao Y]]
-[[Category: Binding protein for cyclosporin some]]
-[[Category: Cyclophilin]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 30 13:57:03 2008''