3qyu: Difference between revisions

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-[[Image:3qyu.png|left|200px]]
-{{STRUCTURE_3qyu|  PDB=3qyu  |  SCENE=  }}
+==Crystal structure of human cyclophilin D at 1.54 A resolution at room temperature==
+<StructureSection load='3qyu' size='340' side='right'caption='[[3qyu]], [[Resolution|resolution]] 1.54&Aring;' scene=''>
-===Crystal structure of human cyclophilin D at 1.54 A resolution at room temperature===
+== Structural highlights ==
+<table><tr><td colspan='2'>[[3qyu]] 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=3QYU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QYU FirstGlance]. <br>
-{{ABSTRACT_PUBMED_21904027}}
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.54&#8491;</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=3qyu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qyu OCA], [https://pdbe.org/3qyu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qyu RCSB], [https://www.ebi.ac.uk/pdbsum/3qyu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qyu ProSAT]</span></td></tr>
-==About this Structure==
+</table>
-[[3qyu]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QYU OCA].
+== Function ==
+[https://www.uniprot.org/uniprot/PPIF_HUMAN PPIF_HUMAN] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Involved in regulation of the mitochondrial permeability transition pore (mPTP). It is proposed that its association with the mPTP is masking a binding site for inhibiting inorganic phosphate (Pi) and promotes the open probablity of the mPTP leading to apoptosis or necrosis; the requirement of the PPIase activity for this function is debated. In cooperation with mitochondrial TP53 is involved in activating oxidative stress-induced necrosis. Involved in modulation of mitochondrial membrane F(1)F(0) ATP synthase activity and regulation of mitochondrial matrix adenine nucleotide levels. Has anti-apoptotic activity independently of mPTP and in cooperation with BCL2 inhibits cytochrome c-dependent apoptosis.<ref>PMID:19228691</ref> <ref>PMID:22726440</ref>
 ==See Also==
-*[[Cyclophilin|Cyclophilin]]
+*[[Cyclophilin 3D structures|Cyclophilin 3D structures]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:021904027</ref><references group="xtra"/>
+__TOC__
+</StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Peptidylprolyl isomerase]]
+[[Category: Large Structures]]
-[[Category: Colliandre, L.]]
+[[Category: Colliandre L]]
-[[Category: Gelin, M.]]
+[[Category: Gelin M]]
-[[Category: Guichou, J F.]]
+[[Category: Guichou J-F]]
-[[Category: Labesse, G.]]
+[[Category: Labesse G]]
-[[Category: Beta barrel]]
-[[Category: Isomerase]]
-[[Category: Mitochondria]]
-[[Category: Prolyl cis/trans isomerase]]