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1rmh

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(New page: 200px<br /><applet load="1rmh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rmh, resolution 2.4&Aring;" /> '''RECOMBINANT CYCLOPHIL...)
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[[Image:1rmh.gif|left|200px]]<br /><applet load="1rmh" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1rmh, resolution 2.4&Aring;" />
 
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'''RECOMBINANT CYCLOPHILIN A FROM HUMAN T CELL'''<br />
 
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==Overview==
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==RECOMBINANT CYCLOPHILIN A FROM HUMAN T CELL==
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The crystal structure of human recombinant cyclophilin A complexed with a, substrate of succinyl-Ala-Ala-Pro-Phe-p-nitroanilide (AAPF) has been, determined and refined to an R-factor of 0.189 at 2.4 A resolution. The, structure revealed only the cis form of the substrate bound to cyclophilin, A in a stoichiometry of 1:1. This binding ratio is different from the, structure of cyclophilin A complexed with the tetrapeptide, N-acetyl-Ala-Ala-Pro-Ala-amidomethylcourmarin. Model docking revealed that, the trans form of AAPF does not fit into the active site. The observation, that only the trans cis form of AAPF binds to cyclophilin A implies that, cyclophilin A predominantly catalyzes the trans to cis isomerization of a, peptidylprolyl amide bond. On the basis of the structure, it is proposed, that Arg55 hydrogen-bonds to the nitrogen to deconjugate the resonance of, the prolyl amide bond and thus facilitates the cis-trans rotation.
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<StructureSection load='1rmh' size='340' side='right'caption='[[1rmh]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1rmh]] is a 4 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=1RMH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RMH 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]] 2.4&#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=NIT:4-NITROANILINE'>NIT</scene>, <scene name='pdbligand=SIN:SUCCINIC+ACID'>SIN</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=1rmh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rmh OCA], [https://pdbe.org/1rmh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rmh RCSB], [https://www.ebi.ac.uk/pdbsum/1rmh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rmh 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/rm/1rmh_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=1rmh 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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1RMH 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RMH 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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Crystal structure implies that cyclophilin predominantly catalyzes the trans to cis isomerization., Zhao Y, Ke H, Biochemistry. 1996 Jun 11;35(23):7356-61. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8652511 8652511]
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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: Ke, H.]]
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[[Category: Ke H]]
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[[Category: Zhao, Y.]]
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[[Category: Zhao Y]]
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[[Category: complex (isomerase/substrate)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:42:40 2007''
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Current revision

RECOMBINANT CYCLOPHILIN A FROM HUMAN T CELL

PDB ID 1rmh

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