4zsd: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
m Protected "4zsd" [edit=sysop:move=sysop]
No edit summary
Line 1: Line 1:
'''Unreleased structure'''
==Human Cyclophilin D Complexed with an Inhibitor at room temperature==
 
<StructureSection load='4zsd' size='340' side='right' caption='[[4zsd]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
The entry 4zsd is ON HOLD
== Structural highlights ==
 
<table><tr><td colspan='2'>[[4zsd]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZSD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ZSD FirstGlance]. <br>
Authors: Gelin, M., Delfosse, V., Allemand, F., Hoh, F., Sallaz-Damaz, Y., Pirocchi, M., Bourguet, W., Ferrer, J.-L., Labesse, G., Guichou, J.-F.
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=7I6:1-(4-AMINOBENZYL)-3-[(2S)-4-(METHYLSULFANYL)-1-{(2R)-2-[2-(METHYLSULFANYL)PHENYL]PYRROLIDIN-1-YL}-1-OXOBUTAN-2-YL]UREA'>7I6</scene></td></tr>
 
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4j5c|4j5c]]</td></tr>
Description: Human Cyclophilin D Complexed with an Inhibitor at room temperature
<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>
[[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=4zsd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zsd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4zsd RCSB], [http://www.ebi.ac.uk/pdbsum/4zsd PDBsum]</span></td></tr>
[[Category: Guichou, J.-F]]
</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: Peptidylprolyl isomerase]]
[[Category: Allemand, F]]
[[Category: Bourguet, W]]
[[Category: Delfosse, V]]
[[Category: Delfosse, V]]
[[Category: Allemand, F]]
[[Category: Ferrer, J L]]
[[Category: Labesse, G]]
[[Category: Sallaz-Damaz, Y]]
[[Category: Gelin, M]]
[[Category: Gelin, M]]
[[Category: Bourguet, W]]
[[Category: Guichou, J F]]
[[Category: Ferrer, J.-L]]
[[Category: Hoh, F]]
[[Category: Hoh, F]]
[[Category: Labesse, G]]
[[Category: Pirocchi, M]]
[[Category: Pirocchi, M]]
[[Category: Sallaz-Damaz, Y]]
[[Category: Isomerase]]
[[Category: Isomerase inhibitor complex]]

Revision as of 17:52, 12 August 2015

Human Cyclophilin D Complexed with an Inhibitor at room temperatureHuman Cyclophilin D Complexed with an Inhibitor at room temperature

Structural highlights

4zsd is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Activity:Peptidylprolyl isomerase, with EC number 5.2.1.8
Resources:FirstGlance, OCA, RCSB, PDBsum

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]

References

  1. Eliseev RA, Malecki J, Lester T, Zhang Y, Humphrey J, Gunter TE. Cyclophilin D interacts with Bcl2 and exerts an anti-apoptotic effect. J Biol Chem. 2009 Apr 10;284(15):9692-9. doi: 10.1074/jbc.M808750200. Epub 2009, Feb 19. PMID:19228691 doi:http://dx.doi.org/10.1074/jbc.M808750200
  2. Vaseva AV, Marchenko ND, Ji K, Tsirka SE, Holzmann S, Moll UM. p53 opens the mitochondrial permeability transition pore to trigger necrosis. Cell. 2012 Jun 22;149(7):1536-48. doi: 10.1016/j.cell.2012.05.014. PMID:22726440 doi:10.1016/j.cell.2012.05.014

4zsd, resolution 1.45Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA