This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


6dun

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (06:14, 11 October 2023) (edit) (undo)
 
(One intermediate revision not shown.)
Line 1: Line 1:
==Crystal Structure Analysis of PIN1==
==Crystal Structure Analysis of PIN1==
-
<StructureSection load='6dun' size='340' side='right' caption='[[6dun]], [[Resolution|resolution]] 1.59&Aring;' scene=''>
+
<StructureSection load='6dun' size='340' side='right'caption='[[6dun]], [[Resolution|resolution]] 1.59&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[6dun]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DUN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6DUN FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[6dun]] is a 2 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=6DUN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6DUN FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TAS:TRIHYDROXYARSENITE(III)'>TAS</scene></td></tr>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.59&#8491;</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 id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TAS:TRIHYDROXYARSENITE(III)'>TAS</scene></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=6dun FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dun OCA], [http://pdbe.org/6dun PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6dun RCSB], [http://www.ebi.ac.uk/pdbsum/6dun PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6dun ProSAT]</span></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=6dun FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dun OCA], [https://pdbe.org/6dun PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6dun RCSB], [https://www.ebi.ac.uk/pdbsum/6dun PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6dun ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== 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>
+
[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>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
Line 19: Line 19:
</div>
</div>
<div class="pdbe-citations 6dun" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 6dun" style="background-color:#fffaf0;"></div>
 +
 +
==See Also==
 +
*[[Peptidyl-prolyl cis-trans isomerase 3D structures|Peptidyl-prolyl cis-trans isomerase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Peptidylprolyl isomerase]]
+
[[Category: Homo sapiens]]
-
[[Category: Dhe-Paganon, S]]
+
[[Category: Large Structures]]
-
[[Category: Seo, H S]]
+
[[Category: Dhe-Paganon S]]
-
[[Category: Isomerase]]
+
[[Category: Seo H-S]]
-
[[Category: Prolyl isomerase]]
+

Current revision

Crystal Structure Analysis of PIN1

PDB ID 6dun

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools