7kjo
From Proteopedia
(Difference between revisions)
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==crystal structure of PLEKHA7 PH domain biding SO4== | ==crystal structure of PLEKHA7 PH domain biding SO4== | ||
| - | <StructureSection load='7kjo' size='340' side='right'caption='[[7kjo]]' scene=''> | + | <StructureSection load='7kjo' size='340' side='right'caption='[[7kjo]], [[Resolution|resolution]] 1.45Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7KJO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7KJO FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7kjo]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7KJO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7KJO FirstGlance]. <br> |
| - | </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=7kjo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7kjo OCA], [https://pdbe.org/7kjo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7kjo RCSB], [https://www.ebi.ac.uk/pdbsum/7kjo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7kjo ProSAT]</span></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PLEKHA7 ([https://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'>[https://proteopedia.org/fgij/fg.htm?mol=7kjo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7kjo OCA], [https://pdbe.org/7kjo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7kjo RCSB], [https://www.ebi.ac.uk/pdbsum/7kjo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7kjo ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[https://www.uniprot.org/uniprot/PKHA7_HUMAN PKHA7_HUMAN]] Required for zonula adherens biogenesis and maintenance (PubMed:19041755). Acts via its interaction with CAMSAP3, which anchors microtubules at their minus-ends to zonula adherens, leading to the recruitment of KIFC3 kinesin to the junctional site (PubMed:19041755). Mediates docking of ADAM10 to zonula adherens through a PDZD11-dependent interaction with the ADAM10-binding protein TSPAN33 (PubMed:30463011).<ref>PMID:19041755</ref> <ref>PMID:30463011</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | PLEKHA7 (pleckstrin homology domain containing family A member 7) plays key roles in intracellular signaling, cytoskeletal organization, and cell adhesion, and is associated with multiple human cancers. The interactions of its pleckstrin homology (PH) domain with membrane phosphatidyl-inositol-phosphate (PIP) lipids are critical for proper cellular localization and function, but little is known about how PLEKHA7 and other PH domains interact with membrane-embedded PIPs. Here we describe the structural basis for recognition of membrane-bound PIPs by PLEHA7. Using X-ray crystallography, nuclear magnetic resonance, molecular dynamics simulations, and isothermal titration calorimetry, we show that the interaction of PLEKHA7 with PIPs is multivalent, distinct from a discrete one-to-one interaction, and induces PIP clustering. Our findings reveal a central role of the membrane assembly in mediating protein-PIP association and provide a roadmap for understanding how the PH domain contributes to the signaling, adhesion, and nanoclustering functions of PLEKHA7. | ||
| + | |||
| + | Structural basis for the association of PLEKHA7 with membrane-embedded phosphatidylinositol lipids.,Aleshin AE, Yao Y, Iftikhar A, Bobkov AA, Yu J, Cadwell G, Klein MG, Dong C, Bankston LA, Liddington RC, Im W, Powis G, Marassi FM Structure. 2021 Apr 13. pii: S0969-2126(21)00116-7. doi:, 10.1016/j.str.2021.03.018. PMID:33878292<ref>PMID:33878292</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7kjo" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Human]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Aleshin | + | [[Category: Aleshin, A E]] |
| - | [[Category: Liddington | + | [[Category: Liddington, R C]] |
| - | [[Category: Marassi | + | [[Category: Marassi, F M]] |
| + | [[Category: Cell adhesion]] | ||
| + | [[Category: Inositol-phosphate]] | ||
| + | [[Category: Ph domain]] | ||
| + | [[Category: Pip]] | ||
| + | [[Category: Pleckstrin homology domain]] | ||
| + | [[Category: Plekha7]] | ||
Revision as of 09:13, 5 May 2021
crystal structure of PLEKHA7 PH domain biding SO4
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