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.

1xx0

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

Structure of the C-terminal PH domain of human pleckstrin

Structural highlights

1xx0 is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1xx0"

@@ Line 1: / Line 1: @@
 ==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 ==
-<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://oca.weizmann.ac.il/oca-docs/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://oca.weizmann.ac.il/oca-docs/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>
 == 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 ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 32: / Line 32: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
-[[Category: Edlich, C]]
+[[Category: Large Structures]]
-[[Category: Muhle-Goll, C]]
+[[Category: Edlich C]]
-[[Category: Sattler, M]]
+[[Category: Muhle-Goll C]]
-[[Category: Simon, B]]
+[[Category: Sattler M]]
-[[Category: Stier, G]]
+[[Category: Simon B]]
-[[Category: C-terminal]]
+[[Category: Stier G]]
-[[Category: Lipid binding protein]]
-[[Category: Ph]]
-[[Category: Pleckstrin]]
-[[Category: Pleckstrin homology]]

1xx0

From Proteopedia

Current revision

Structure of the C-terminal PH domain of human pleckstrin

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox