4j58: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Human Cyclophilin D Complexed with an Inhibitor== | ==Human Cyclophilin D Complexed with an Inhibitor== | ||
<StructureSection load='4j58' size='340' side='right' caption='[[4j58]], [[Resolution|resolution]] 1.28Å' scene=''> | <StructureSection load='4j58' size='340' side='right' caption='[[4j58]], [[Resolution|resolution]] 1.28Å' scene=''> | ||
| Line 7: | Line 8: | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CYP3, PPIF ([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">CYP3, PPIF ([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=4j58 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j58 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4j58 RCSB], [http://www.ebi.ac.uk/pdbsum/4j58 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=4j58 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j58 OCA], [http://pdbe.org/4j58 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4j58 RCSB], [http://www.ebi.ac.uk/pdbsum/4j58 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4j58 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
Revision as of 18:13, 5 August 2016
Human Cyclophilin D Complexed with an InhibitorHuman Cyclophilin D Complexed with an Inhibitor
Structural highlights
Function[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.[1] [2] See AlsoReferences
|
| ||||||||||||||||||||||