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1vbs

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[[Image:1vbs.gif|left|200px]]<br /><applet load="1vbs" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1vbs, resolution 2.0&Aring;" />
 
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'''STRUCTURE OF CYCLOPHILIN COMPLEXED WITH (D)ALA CONTAINING TETRAPEPTIDE'''<br />
 
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==Overview==
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==STRUCTURE OF CYCLOPHILIN COMPLEXED WITH (D)ALA CONTAINING TETRAPEPTIDE==
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The stereospecificity of peptidyl prolyl cis/trans isomerases (PPIases) was studied using tetrapeptide substrate analogs in which one amino acid residue was replaced by the cognate D-amino acid in various positions of the peptide chain. Reversed stereocenters around proline markedly increased the rate of the spontaneous trans to cis isomerization of the prolyl bond whereas cis to trans isomerizations were less sensitive. PPIases like human cyclophilin18, human FKBP12, Escherichia coli parvulin10 and the PPIase domain of E. coli trigger factor exhibited stereoselectivity demanding at the P1 to P2' position of the substrate chain. The discriminating factor for stereoselectivity was the lack of formation of the Michaelis complexes of the diastereomeric substrates. However, D-alanine at the P1 position preserved considerable affinity to the active site, and largely prevented activation of the catalytic machinery for all PPIases investigated.
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<StructureSection load='1vbs' size='340' side='right'caption='[[1vbs]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1vbs]] 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=1VBS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VBS FirstGlance]. <br>
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</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&#8491;</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=DAL:D-ALANINE'>DAL</scene>, <scene name='pdbligand=NIT:4-NITROANILINE'>NIT</scene></td></tr>
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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=1vbs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vbs OCA], [https://pdbe.org/1vbs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vbs RCSB], [https://www.ebi.ac.uk/pdbsum/1vbs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vbs ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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.
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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/vb/1vbs_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1vbs ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1VBS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VBS OCA].
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*[[Cyclophilin 3D structures|Cyclophilin 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Mapping the stereospecificity of peptidyl prolyl cis/trans isomerases., Schiene C, Reimer U, Schutkowski M, Fischer G, FEBS Lett. 1998 Aug 7;432(3):202-6. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9720925 9720925]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Chen, Y.]]
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[[Category: Chen Y]]
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[[Category: Fischer, G.]]
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[[Category: Fischer G]]
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[[Category: Ke, H.]]
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[[Category: Ke H]]
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[[Category: Schutkowski, M.]]
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[[Category: Schutkowski M]]
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[[Category: Zhao, Y.]]
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[[Category: Zhao Y]]
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[[Category: competitive inhibitor]]
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[[Category: complex (isomerase/peptide)]]
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[[Category: cyclophilin a]]
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[[Category: mechanism]]
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[[Category: peptidyl-prolyl isomerase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:33:33 2008''
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Current revision

STRUCTURE OF CYCLOPHILIN COMPLEXED WITH (D)ALA CONTAINING TETRAPEPTIDE

PDB ID 1vbs

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