3cyh: Difference between revisions

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New page: left|200px<br /><applet load="3cyh" size="450" color="white" frame="true" align="right" spinBox="true" caption="3cyh, resolution 1.9Å" /> '''CYCLOPHILIN A COMPLEX...
 
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[[Image:3cyh.gif|left|200px]]<br /><applet load="3cyh" size="450" color="white" frame="true" align="right" spinBox="true"
caption="3cyh, resolution 1.9&Aring;" />
'''CYCLOPHILIN A COMPLEXED WITH DIPEPTIDE SER-PRO'''<br />


==Overview==
==CYCLOPHILIN A COMPLEXED WITH DIPEPTIDE SER-PRO==
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.
<StructureSection load='3cyh' size='340' side='right'caption='[[3cyh]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3cyh]] 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=3CYH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CYH FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PRO:PROLINE'>PRO</scene>, <scene name='pdbligand=SER:SERINE'>SER</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3cyh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cyh OCA], [https://pdbe.org/3cyh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3cyh RCSB], [https://www.ebi.ac.uk/pdbsum/3cyh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3cyh 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/3cyh_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=3cyh ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
3CYH 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=3CYH OCA].
*[[Cyclophilin 3D structures|Cyclophilin 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Mechanistic implication of crystal structures of the cyclophilin-dipeptide complexes., Zhao Y, Ke H, Biochemistry. 1996 Jun 11;35(23):7362-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8652512 8652512]
[[Category: Homo sapiens]]
[[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 a]]
[[Category: complex]]
[[Category: cyclophilin]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:38:25 2007''

Latest revision as of 12:39, 21 February 2024

CYCLOPHILIN A COMPLEXED WITH DIPEPTIDE SER-PROCYCLOPHILIN A COMPLEXED WITH DIPEPTIDE SER-PRO

Structural highlights

3cyh is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.9Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PPIA_HUMAN PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

3cyh, resolution 1.90Å

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