5cbv: Difference between revisions

Line 1:

~~'''Unreleased structure'''~~

~~The entry~~ 5cbv is ~~ON HOLD~~ ~~until Paper Publication~~

==Human Cyclophilin D Complexed with Inhibitor==

~~Authors~~:

== Structural highlights ==

<table><tr><td colspan='2'>[[5cbv]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CBV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CBV FirstGlance]. <br>

~~Description~~:

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=4ZP:ETHYL+N-{[3-(PYRIDIN-3-YL)BENZYL]CARBAMOYL}GLYCINATE'>4ZP</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr>

[[Category: ~~Unreleased Structures~~]]

<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=5cbv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cbv OCA], [http://pdbe.org/5cbv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5cbv RCSB], [http://www.ebi.ac.uk/pdbsum/5cbv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5cbv ProSAT]</span></td></tr>

</table>

== Function ==

[[http://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>

== References ==

__TOC__

</StructureSection>

[[Category: Awais, M]]

[[Category: Berry, N]]

[[Category: Gibson, R P]]

[[Category: Javed, A]]

[[Category: Kershaw, N]]

[[Category: Latawiec, D]]

[[Category: Lian, L Y]]

[[Category: Neill, P O]]

[[Category: Pandalaneni, S]]

[[Category: Shore, E]]

[[Category: Sutton, R]]

[[Category: Wen, L]]

[[Category: Complex]]

[[Category: Cyclophilin]]

[[Category: Inhibitor]]

[[Category: Isomerase]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 5cbv is ON HOLD  until Paper Publication
+==Human Cyclophilin D Complexed with Inhibitor==
+<StructureSection load='5cbv' size='340' side='right' caption='[[5cbv]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
-Authors:
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5cbv]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CBV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CBV FirstGlance]. <br>
-Description:
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=4ZP:ETHYL+N-{[3-(PYRIDIN-3-YL)BENZYL]CARBAMOYL}GLYCINATE'>4ZP</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr>
-[[Category: Unreleased Structures]]
+<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=5cbv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cbv OCA], [http://pdbe.org/5cbv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5cbv RCSB], [http://www.ebi.ac.uk/pdbsum/5cbv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5cbv ProSAT]</span></td></tr>
+</table>
+== Function ==
+[[http://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>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Awais, M]]
+[[Category: Berry, N]]
+[[Category: Gibson, R P]]
+[[Category: Javed, A]]
+[[Category: Kershaw, N]]
+[[Category: Latawiec, D]]
+[[Category: Lian, L Y]]
+[[Category: Neill, P O]]
+[[Category: Pandalaneni, S]]
+[[Category: Shore, E]]
+[[Category: Sutton, R]]
+[[Category: Wen, L]]
+[[Category: Complex]]
+[[Category: Cyclophilin]]
+[[Category: Inhibitor]]
+[[Category: Isomerase]]