2cyh: Difference between revisions
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==CYCLOPHILIN A COMPLEXED WITH DIPEPTIDE ALA-PRO== | ==CYCLOPHILIN A COMPLEXED WITH DIPEPTIDE ALA-PRO== | ||
<StructureSection load='2cyh' size='340' side='right' caption='[[2cyh]], [[Resolution|resolution]] 1.64Å' scene=''> | <StructureSection load='2cyh' size='340' side='right' caption='[[2cyh]], [[Resolution|resolution]] 1.64Å' scene=''> | ||
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CYCLOPHILIN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CYCLOPHILIN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2cyh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cyh OCA], [http://pdbe.org/2cyh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2cyh RCSB], [http://www.ebi.ac.uk/pdbsum/2cyh PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2cyh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cyh OCA], [http://pdbe.org/2cyh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2cyh RCSB], [http://www.ebi.ac.uk/pdbsum/2cyh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2cyh ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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</div> | </div> | ||
<div class="pdbe-citations 2cyh" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 2cyh" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 10:06, 29 November 2017
CYCLOPHILIN A COMPLEXED WITH DIPEPTIDE ALA-PROCYCLOPHILIN A COMPLEXED WITH DIPEPTIDE ALA-PRO
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. Mechanistic implication of crystal structures of the cyclophilin-dipeptide complexes.,Zhao Y, Ke H Biochemistry. 1996 Jun 11;35(23):7362-8. PMID:8652512[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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