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| | ==Structure of the C-terminal PH domain of human pleckstrin== | | ==Structure of the C-terminal PH domain of human pleckstrin== |
| - | <StructureSection load='1xx0' size='340' side='right'caption='[[1xx0]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | + | <StructureSection load='1xx0' size='340' side='right'caption='[[1xx0]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1xx0]] 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=1XX0 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1XX0 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1xx0]] 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=1XX0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XX0 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PLEK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1xx0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xx0 OCA], [http://pdbe.org/1xx0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1xx0 RCSB], [http://www.ebi.ac.uk/pdbsum/1xx0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1xx0 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=1xx0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xx0 OCA], [https://pdbe.org/1xx0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xx0 RCSB], [https://www.ebi.ac.uk/pdbsum/1xx0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xx0 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PLEK_HUMAN PLEK_HUMAN]] Major protein kinase C substrate of platelets. | + | [https://www.uniprot.org/uniprot/PLEK_HUMAN PLEK_HUMAN] Major protein kinase C substrate of platelets. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Edlich, C]] | + | [[Category: Edlich C]] |
| - | [[Category: Muhle-Goll, C]] | + | [[Category: Muhle-Goll C]] |
| - | [[Category: Sattler, M]] | + | [[Category: Sattler M]] |
| - | [[Category: Simon, B]] | + | [[Category: Simon B]] |
| - | [[Category: Stier, G]] | + | [[Category: Stier G]] |
| - | [[Category: C-terminal]]
| + | |
| - | [[Category: Lipid binding protein]]
| + | |
| - | [[Category: Ph]]
| + | |
| - | [[Category: Pleckstrin]]
| + | |
| - | [[Category: Pleckstrin homology]]
| + | |
| Structural highlights
Function
PLEK_HUMAN Major protein kinase C substrate of platelets.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Pleckstrin is the major target of protein kinase C (PKC) in blood platelets. Its phosphorylation triggers responses that ultimately lead to platelet activation and blood clot formation. Pleckstrin consists of three domains: a pleckstrin homology (PH) domain at both termini and a central DEP (Dishevelled, Egl-1, Pleckstrin) domain. Here, we report the solution nuclear magnetic resonance (NMR) structure of the C-terminal PH domain (C-PH) of human pleckstrin-1. We show that this PH domain binds phosphatidylinositol-3,4-bisphosphate (PtdIns(3,4)P2) with high specificity in protein lipid overlay assays. Using NMR titration experiments and mutational analysis, residues involved in binding to PtdIns(3,4)P2 are identified. The binding site is formed by a patch of basic residues from the beta1 and beta2 strands and the beta1-beta2 loop. Since PtdIns(3,4)P2 is an important signaling molecule in platelets, our data suggest a C-PH dependent regulation of pleckstrin function in response to PtdIns(3,4)P2.
Structure and phosphatidylinositol-(3,4)-bisphosphate binding of the C-terminal PH domain of human pleckstrin.,Edlich C, Stier G, Simon B, Sattler M, Muhle-Goll C Structure. 2005 Feb;13(2):277-86. PMID:15698571[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Edlich C, Stier G, Simon B, Sattler M, Muhle-Goll C. Structure and phosphatidylinositol-(3,4)-bisphosphate binding of the C-terminal PH domain of human pleckstrin. Structure. 2005 Feb;13(2):277-86. PMID:15698571 doi:10.1016/j.str.2004.11.012
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