1ynd

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(New page: 200px<br /> <applet load="1ynd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ynd, resolution 1.60&Aring;" /> '''Structure of human ...)
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[[Image:1ynd.gif|left|200px]]<br />
 
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<applet load="1ynd" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ynd, resolution 1.60&Aring;" />
 
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'''Structure of human cyclophilin A in complex with the novel immunosuppressant sanglifehrin A at 1.6A resolution'''<br />
 
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==Overview==
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==Structure of human cyclophilin A in complex with the novel immunosuppressant sanglifehrin A at 1.6A resolution==
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Sanglifehrin A (SFA) is a novel immunosuppressant isolated from, Streptomyces sp. that binds strongly to the human immunophilin cyclophilin, A (CypA). SFA exerts its immunosuppressive activity through a mode of, action different from that of all other known immunophilin-binding, substances, namely cyclosporine A (CsA), FK506, and rapamycin. We have, determined the crystal structure of human CypA in complex with SFA at 1.6, A resolution. The high resolution of the structure revealed the absolute, configuration at all 17 chiral centers of SFA as well as the details of, the CypA/SFA interactions. In particular, it was shown that the, 22-membered macrocycle of SFA is deeply embedded in the same binding site, as CsA and forms six direct hydrogen bonds with CypA. The effector domain, of SFA, on the other hand, has a chemical and three-dimensional structure, very different from CsA, already strongly suggesting different, immunosuppressive mechanisms. Furthermore, two CypA.SFA complexes form a, dimer in the crystal as well as in solution as shown by light scattering, and size exclusion chromatography experiments. This observation raises the, possibility that the dimer of CypA.SFA complexes is the molecular species, mediating the immunosuppressive effect.
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<StructureSection load='1ynd' size='340' side='right'caption='[[1ynd]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1ynd]] 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=1YND OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YND 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]] 1.6&#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=SFA:SANGLIFEHRIN+A'>SFA</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=1ynd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ynd OCA], [https://pdbe.org/1ynd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ynd RCSB], [https://www.ebi.ac.uk/pdbsum/1ynd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ynd 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/yn/1ynd_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=1ynd ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Sanglifehrin A (SFA) is a novel immunosuppressant isolated from Streptomyces sp. that binds strongly to the human immunophilin cyclophilin A (CypA). SFA exerts its immunosuppressive activity through a mode of action different from that of all other known immunophilin-binding substances, namely cyclosporine A (CsA), FK506, and rapamycin. We have determined the crystal structure of human CypA in complex with SFA at 1.6 A resolution. The high resolution of the structure revealed the absolute configuration at all 17 chiral centers of SFA as well as the details of the CypA/SFA interactions. In particular, it was shown that the 22-membered macrocycle of SFA is deeply embedded in the same binding site as CsA and forms six direct hydrogen bonds with CypA. The effector domain of SFA, on the other hand, has a chemical and three-dimensional structure very different from CsA, already strongly suggesting different immunosuppressive mechanisms. Furthermore, two CypA.SFA complexes form a dimer in the crystal as well as in solution as shown by light scattering and size exclusion chromatography experiments. This observation raises the possibility that the dimer of CypA.SFA complexes is the molecular species mediating the immunosuppressive effect.
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==About this Structure==
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Structure of human cyclophilin A in complex with the novel immunosuppressant sanglifehrin A at 1.6 A resolution.,Kallen J, Sedrani R, Zenke G, Wagner J J Biol Chem. 2005 Jun 10;280(23):21965-71. Epub 2005 Mar 16. PMID:15772070<ref>PMID:15772070</ref>
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1YND is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with SFA as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1YND OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Structure of human cyclophilin A in complex with the novel immunosuppressant sanglifehrin A at 1.6 A resolution., Kallen J, Sedrani R, Zenke G, Wagner J, J Biol Chem. 2005 Jun 10;280(23):21965-71. Epub 2005 Mar 16. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15772070 15772070]
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</div>
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[[Category: Homo sapiens]]
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<div class="pdbe-citations 1ynd" style="background-color:#fffaf0;"></div>
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[[Category: Peptidylprolyl isomerase]]
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[[Category: Single protein]]
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[[Category: Kallen, J.]]
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[[Category: Sedrani, R.]]
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[[Category: Wagner, J.]]
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[[Category: Zenke, G.]]
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[[Category: SFA]]
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[[Category: beta sandwich]]
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[[Category: cyclophilin-ligand complex]]
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[[Category: cyclosporin]]
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[[Category: isomerase]]
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[[Category: rotamase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:21:52 2007''
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==See Also==
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*[[Cyclophilin 3D structures|Cyclophilin 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Kallen J]]
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[[Category: Sedrani R]]
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[[Category: Wagner J]]
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[[Category: Zenke G]]

Current revision

Structure of human cyclophilin A in complex with the novel immunosuppressant sanglifehrin A at 1.6A resolution

PDB ID 1ynd

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