6vro
From Proteopedia
(Difference between revisions)
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<StructureSection load='6vro' size='340' side='right'caption='[[6vro]], [[Resolution|resolution]] 2.45Å' scene=''> | <StructureSection load='6vro' size='340' side='right'caption='[[6vro]], [[Resolution|resolution]] 2.45Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6vro]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VRO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6VRO FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6vro]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VRO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6VRO FirstGlance]. <br> |
| - | </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=6vro FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vro OCA], [http://pdbe.org/6vro PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6vro RCSB], [http://www.ebi.ac.uk/pdbsum/6vro PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6vro ProSAT]</span></td></tr> | + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PPP2R5C, KIAA0044 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=6vro FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vro OCA], [http://pdbe.org/6vro PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6vro RCSB], [http://www.ebi.ac.uk/pdbsum/6vro PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6vro ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/2A5G_HUMAN 2A5G_HUMAN]] The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment. The PP2A-PPP2R5C holoenzyme may specifically dephosphorylate and activate TP53 and play a role in DNA damage-induced inhibition of cell proliferation. PP2A-PPP2R5C may also regulate the ERK signaling pathway through ERK dephosphorylation.<ref>PMID:16456541</ref> <ref>PMID:17245430</ref> [[http://www.uniprot.org/uniprot/CRBG1_HUMAN CRBG1_HUMAN]] May function as suppressor of malignant melanoma. It may exert its effects through interactions with the cytoskeleton. | [[http://www.uniprot.org/uniprot/2A5G_HUMAN 2A5G_HUMAN]] The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment. The PP2A-PPP2R5C holoenzyme may specifically dephosphorylate and activate TP53 and play a role in DNA damage-induced inhibition of cell proliferation. PP2A-PPP2R5C may also regulate the ERK signaling pathway through ERK dephosphorylation.<ref>PMID:16456541</ref> <ref>PMID:17245430</ref> [[http://www.uniprot.org/uniprot/CRBG1_HUMAN CRBG1_HUMAN]] May function as suppressor of malignant melanoma. It may exert its effects through interactions with the cytoskeleton. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The recruitment of substrates by the ser/thr protein phosphatase 2A (PP2A) is poorly understood, limiting our understanding of PP2A-regulated signaling. Recently, the first PP2A:B56 consensus binding motif, LxxIxE, was identified. However, most validated LxxIxE motifs bind PP2A:B56 with micromolar affinities, suggesting that additional motifs exist to enhance PP2A:B56 binding. Here, we report the requirement of a positively charged motif in a subset of PP2A:B56 interactors, including KIF4A, to facilitate B56 binding via dynamic, electrostatic interactions. Using molecular and cellular experiments, we show that a conserved, negatively charged groove on B56 mediates dynamic binding. We also discovered that this positively charged motif, in addition to facilitating KIF4A dephosphorylation, is essential for condensin I binding, a function distinct and exclusive from PP2A-B56 binding. Together, these results reveal how dynamic, charge-charge interactions fine-tune the interactions mediated by specific motifs, providing a new framework for understanding how PP2A regulation drives cellular signaling. | ||
| + | |||
| + | A dynamic charge-charge interaction modulates PP2A:B56 substrate recruitment.,Wang X, Garvanska DH, Nasa I, Ueki Y, Zhang G, Kettenbach AN, Peti W, Nilsson J, Page R Elife. 2020 Mar 20;9. pii: 55966. doi: 10.7554/eLife.55966. PMID:32195664<ref>PMID:32195664</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6vro" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Human]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Page, R]] | [[Category: Page, R]] | ||
Revision as of 09:49, 1 April 2020
The structure of the PP2A B56 subunit AIM1 complex
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Categories: Human | Large Structures | Page, R | Peti, W | Wang, X | Complex | Hydrolase | Ser/thr phosphatase
