4gwt
From Proteopedia
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- | {{STRUCTURE_4gwt| PDB=4gwt | SCENE= }} | ||
- | ===Structure of racemic Pin1 WW domain cocrystallized with DL-malic acid=== | ||
- | {{ABSTRACT_PUBMED_24311591}} | ||
- | == | + | ==Structure of racemic Pin1 WW domain cocrystallized with DL-malic acid== |
- | [[http://www.uniprot.org/uniprot/PIN1_HUMAN PIN1_HUMAN | + | <StructureSection load='4gwt' size='340' side='right'caption='[[4gwt]], [[Resolution|resolution]] 2.25Å' scene=''> |
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[4gwt]] 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=4GWT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GWT FirstGlance]. <br> | ||
+ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.25Å</td></tr> | ||
+ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LMR:(2S)-2-HYDROXYBUTANEDIOIC+ACID'>LMR</scene></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=4gwt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gwt OCA], [https://pdbe.org/4gwt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gwt RCSB], [https://www.ebi.ac.uk/pdbsum/4gwt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gwt ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [https://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> | ||
- | == | + | ==See Also== |
- | [[ | + | *[[Peptidyl-prolyl cis-trans isomerase 3D structures|Peptidyl-prolyl cis-trans isomerase 3D structures]] |
- | + | == References == | |
- | == | + | <references/> |
- | + | __TOC__ | |
- | [[Category: | + | </StructureSection> |
- | [[Category: | + | [[Category: Homo sapiens]] |
- | [[Category: | + | [[Category: Large Structures]] |
- | [[Category: | + | [[Category: Forest KT]] |
- | [[Category: | + | [[Category: Gellman SH]] |
- | [[Category: | + | [[Category: Mortenson DE]] |
- | + | [[Category: Yun HG]] | |
- | + | ||
- | + |
Current revision
Structure of racemic Pin1 WW domain cocrystallized with DL-malic acid
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