2cpl

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(New page: 200px<br /> <applet load="2cpl" size="450" color="white" frame="true" align="right" spinBox="true" caption="2cpl, resolution 1.63&Aring;" /> '''SIMILARITIES AND DI...)
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[[Image:2cpl.gif|left|200px]]<br />
 
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<applet load="2cpl" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2cpl, resolution 1.63&Aring;" />
 
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'''SIMILARITIES AND DIFFERENCES BETWEEN HUMAN CYCLOPHILIN A AND OTHER BETA-BARREL STRUCTURES. STRUCTURAL REFINEMENT AT 1.63 ANGSTROMS RESOLUTION'''<br />
 
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==Overview==
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==SIMILARITIES AND DIFFERENCES BETWEEN HUMAN CYCLOPHILIN A AND OTHER BETA-BARREL STRUCTURES. STRUCTURAL REFINEMENT AT 1.63 ANGSTROMS RESOLUTION==
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The structure of the unligated recombinant human cyclophilin A (CyP A) has, been refined to an R-factor of 0.18 at 1.63 A resolution. The, root-mean-squared deviations of the refined structure are 0.013 A and 2.50, degrees from ideal geometries of bond length and bond angle, respectively., Eight antiparallel beta-strands of CyP A form a right-handed beta-barrel., The structure of CyP A is compared with other members in the antiparallel, eight-stranded beta-barrel family and with the parallel eight-stranded, alpha/beta barrels. Although all known eight-stranded barrels are, right-handed, the tilted angle of the strands against the barrel axis, varies from 45 degrees for retinol binding protein and 49 degrees for CyP, A to 70 degrees for superoxide dismutase. As a result, the beta-barrel of, CyP A is not completely superimposable with other members of beta-barrels., The structure of CyP A has a unique topology, distinct from other members, in the beta-barrel family. In addition, CyP A is a closed beta-barrel so, that neither the immunosuppressive drug cyclosporin A (CsA) nor the, proline-containing substrate can bind to the hydrophobic core of the CyP A, barrel, while the hydrophobic core of most other barrels is open for, ligation. These observations probably indicate that CyP A is neither, functionally nor evolutionally related to other beta-barrel structures., Details of interactions between solvent molecules and the active site, residues of CyP A are illustrated. A water-co-operated mechanism, where, the cis&lt;--&gt;trans isomerization might possibly consist of (1) transition of, the prolyl bond and (2) release of N or C-terminal residues of substrate, from CyP, is addressed. The refined structure reveals no disulfide bridges, in CyP A. Cys115 is near the CsA site, but unlikely to be directly, involved in CsA binding because of steric hindrance from Thr119 and, Leu122. This geometry probably rules out any mechanisms involving a, tetrahedral intermediate formed between cysteine and substrate during, cis&lt;--&gt;trans isomerization.
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<StructureSection load='2cpl' size='340' side='right'caption='[[2cpl]], [[Resolution|resolution]] 1.63&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2cpl]] is a 1 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=2CPL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CPL 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]] 1.63&#8491;</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=2cpl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cpl OCA], [https://pdbe.org/2cpl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cpl RCSB], [https://www.ebi.ac.uk/pdbsum/2cpl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cpl 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/cp/2cpl_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=2cpl 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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2CPL 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=2CPL 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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Similarities and differences between human cyclophilin A and other beta-barrel structures. Structural refinement at 1.63 A resolution., Ke H, J Mol Biol. 1992 Nov 20;228(2):539-50. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=1453463 1453463]
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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: isomerase(peptidyl-prolyl cis-trans)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 21:19:14 2007''
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SIMILARITIES AND DIFFERENCES BETWEEN HUMAN CYCLOPHILIN A AND OTHER BETA-BARREL STRUCTURES. STRUCTURAL REFINEMENT AT 1.63 ANGSTROMS RESOLUTION

PDB ID 2cpl

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