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4tyo
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4tyo]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TYO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4TYO FirstGlance]. <br> | <table><tr><td colspan='2'>[[4tyo]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TYO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4TYO FirstGlance]. <br> | ||
| - | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=39X:3-(6-FLUORO-1H-BENZIMIDAZOL-2-YL)-N-(NAPHTHALEN-2-YLCARBONYL)-D-ALANINE'>39X</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>< | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=39X:3-(6-FLUORO-1H-BENZIMIDAZOL-2-YL)-N-(NAPHTHALEN-2-YLCARBONYL)-D-ALANINE'>39X</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3i6c|3i6c]], [[3jyj|3jyj]], [[3ikg|3ikg]], [[3ik8|3ik8]], [[3ikd|3ikd]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3i6c|3i6c]], [[3jyj|3jyj]], [[3ikg|3ikg]], [[3ik8|3ik8]], [[3ikd|3ikd]]</td></tr> |
| - | <tr><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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4tyo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tyo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4tyo RCSB], [http://www.ebi.ac.uk/pdbsum/4tyo 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=4tyo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tyo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4tyo RCSB], [http://www.ebi.ac.uk/pdbsum/4tyo PDBsum]</span></td></tr> |
| - | <table> | + | </table> |
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/PIN1_HUMAN PIN1_HUMAN]] Essential PPIase that regulates mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity. Displays a preference for an acidic residue N-terminal to the isomerized proline bond. Catalyzes pSer/Thr-Pro cis/trans isomerizations. Down-regulates kinase activity of BTK. Can transactivate multiple oncogenes and induce centrosome amplification, chromosome instability and cell transformation. Required for the efficient dephosphorylation and recycling of RAF1 after mitogen activation.<ref>PMID:15664191</ref> <ref>PMID:16644721</ref> <ref>PMID:21497122</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Peptidylprolyl isomerase]] | [[Category: Peptidylprolyl isomerase]] | ||
| - | [[Category: Ferre, R A | + | [[Category: Ferre, R A]] |
| - | [[Category: Greasley, S E | + | [[Category: Greasley, S E]] |
[[Category: Cell cycle]] | [[Category: Cell cycle]] | ||
[[Category: Isomerase]] | [[Category: Isomerase]] | ||
Revision as of 03:43, 25 December 2014
PPIase in complex with a non-phosphate small molecule inhibitor.
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