4tns: Difference between revisions

Line 1:

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

==Structure of Pin1 PPIase domain bound with all-trans retinoic acid==

~~The entry~~ 4tns is ~~ON HOLD until Paper Publication~~

== Structural highlights ==

<table><tr><td colspan='2'>[[4tns]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TNS OCA]. For a guided tour on the structure components use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4TNS FirstGlance].

~~Authors~~: Li, W.Z., ~~Zhang~~, Y.

</td></tr><tr id='ligand'><td class="sblockLbl">[[Ligand|Ligands:]]</td><td class="sblockDat"><scene name='pdbligand=3KV:RETINOIC+ACID'>3KV</scene></td></tr>

<tr id='activity'><td class="sblockLbl">Activity:</td><td class="sblockDat">[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] </td></tr>

~~Description~~: ~~Structure of Pin1~~ PPIase ~~domain bound~~ with ~~all~~-trans ~~retinoic acid~~

<tr id='resources'><td class="sblockLbl">Resources:</td><td class="sblockDat">[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4tns FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tns OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4tns RCSB], [http://www.ebi.ac.uk/pdbsum/4tns PDBsum]</td></tr>

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

</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>

== References ==

__TOC__

</StructureSection>

[[Category: Peptidylprolyl isomerase]]

[[Category: Li, W Z]]

[[Category: Zhang, Y]]

[[Category: ~~Li, W.Z~~]]

[[Category: Isomerase]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+==Structure of Pin1 PPIase domain bound with all-trans retinoic acid==
+<StructureSection load='4tns' size='340' side='right' caption='[[4tns]], [[Resolution|resolution]] 1.33&Aring;' scene=''>
-The entry 4tns is ON HOLD  until Paper Publication
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4tns]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TNS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4TNS FirstGlance]. <br>
-Authors: Li, W.Z., Zhang, Y.
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=3KV:RETINOIC+ACID'>3KV</scene></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>
-Description: Structure of Pin1 PPIase domain bound with all-trans retinoic acid
+<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=4tns FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tns OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4tns RCSB], [http://www.ebi.ac.uk/pdbsum/4tns PDBsum]</span></td></tr>
-[[Category: Unreleased Structures]]
+</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>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Peptidylprolyl isomerase]]
+[[Category: Li, W Z]]
 [[Category: Zhang, Y]]
-[[Category: Li, W.Z]]
+[[Category: Isomerase]]