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.


6sve

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (11:02, 14 June 2023) (edit) (undo)
 
(One intermediate revision not shown.)
Line 1: Line 1:
==Protein allostery of the WW domain at atomic resolution: pCdc25C bound structure==
==Protein allostery of the WW domain at atomic resolution: pCdc25C bound structure==
-
<StructureSection load='6sve' size='340' side='right'caption='[[6sve]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+
<StructureSection load='6sve' size='340' side='right'caption='[[6sve]]' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[6sve]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SVE OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6SVE FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[6sve]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SVE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6SVE FirstGlance]. <br>
-
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6svc|6svc]], [[6svh|6svh]]</td></tr>
+
</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=6sve FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sve OCA], [https://pdbe.org/6sve PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6sve RCSB], [https://www.ebi.ac.uk/pdbsum/6sve PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6sve ProSAT]</span></td></tr>
-
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PIN1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6sve FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sve OCA], [http://pdbe.org/6sve PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6sve RCSB], [http://www.ebi.ac.uk/pdbsum/6sve PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6sve 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 24: Line 21:
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Human]]
+
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Peptidylprolyl isomerase]]
+
[[Category: Friedmann M]]
-
[[Category: Friedmann, M]]
+
[[Category: Guntert P]]
-
[[Category: Guntert, P]]
+
[[Category: Orts J]]
-
[[Category: Orts, J]]
+
[[Category: Riek R]]
-
[[Category: Riek, R]]
+
[[Category: Strotz D]]
-
[[Category: Strotz, D]]
+
[[Category: Vogeli B]]
-
[[Category: Vogeli, B]]
+
-
[[Category: Peptide binding protein]]
+
-
[[Category: Structure from cyana 3 98 12]]
+

Current revision

Protein allostery of the WW domain at atomic resolution: pCdc25C bound structure

PDB ID 6sve

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6sve"
Personal tools