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2adz

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solution structure of the joined PH domain of alpha1-syntrophin

Structural highlights

2adz is a 1 chain structure with sequence from Mus musculus. 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

SNTA1_MOUSE Adapter protein that binds to and probably organizes the subcellular localization of a variety of membrane proteins. May link various receptors to the actin cytoskeleton and the extracellular matrix via the dystrophin glycoprotein complex. Plays an important role in synapse formation and in the organization of UTRN and acetylcholine receptors at the neuromuscular synapse. Binds to phosphatidylinositol 4,5-bisphosphate.

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 homology (PH) domains play diverse roles in cytoskeletal dynamics and signal transduction. Split PH domains represent a unique subclass of PH domains that have been implicated in interactions with complementary partial PH domains 'hidden' in many proteins. Whether partial PH domains exist as independent structural units alone and whether two halves of a split PH domain can fold together to form an intact PH domain are not known. Here, we solved the structure of the PH(N)-PDZ-PH(C) tandem of alpha-syntrophin. The split PH domain of alpha-syntrophin adopts a canonical PH domain fold. The isolated partial PH domains of alpha-syntrophin, although completely unfolded, remain soluble in solution. Mixing of the two isolated domains induces de novo folding and yields a stable PH domain. Our results demonstrate that two complementary partial PH domains are capable of binding to each other to form an intact PH domain. We further showed that the PH(N)-PDZ-PH(C) tandem forms a functionally distinct supramodule, in which the split PH domain and the PDZ domain function synergistically in binding to inositol phospholipids.

Structure of the split PH domain and distinct lipid-binding properties of the PH-PDZ supramodule of alpha-syntrophin.,Yan J, Wen W, Xu W, Long JF, Adams ME, Froehner SC, Zhang M EMBO J. 2005 Dec 7;24(23):3985-95. Epub 2005 Oct 27. PMID:16252003^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Yan J, Wen W, Xu W, Long JF, Adams ME, Froehner SC, Zhang M. Structure of the split PH domain and distinct lipid-binding properties of the PH-PDZ supramodule of alpha-syntrophin. EMBO J. 2005 Dec 7;24(23):3985-95. Epub 2005 Oct 27. PMID:16252003

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2adz"

@@ Line 1: / Line 1: @@
 ==solution structure of the joined PH domain of alpha1-syntrophin==
-<StructureSection load='2adz' size='340' side='right' caption='[[2adz]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='2adz' size='340' side='right'caption='[[2adz]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2adz]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ADZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ADZ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2adz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ADZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ADZ FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1z87|1z87]]</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=2adz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2adz OCA], [http://pdbe.org/2adz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2adz RCSB], [http://www.ebi.ac.uk/pdbsum/2adz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2adz 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=2adz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2adz OCA], [https://pdbe.org/2adz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2adz RCSB], [https://www.ebi.ac.uk/pdbsum/2adz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2adz ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/SNTA1_MOUSE SNTA1_MOUSE]] Adapter protein that binds to and probably organizes the subcellular localization of a variety of membrane proteins. May link various receptors to the actin cytoskeleton and the extracellular matrix via the dystrophin glycoprotein complex. Plays an important role in synapse formation and in the organization of UTRN and acetylcholine receptors at the neuromuscular synapse. Binds to phosphatidylinositol 4,5-bisphosphate.
+[https://www.uniprot.org/uniprot/SNTA1_MOUSE SNTA1_MOUSE] Adapter protein that binds to and probably organizes the subcellular localization of a variety of membrane proteins. May link various receptors to the actin cytoskeleton and the extracellular matrix via the dystrophin glycoprotein complex. Plays an important role in synapse formation and in the organization of UTRN and acetylcholine receptors at the neuromuscular synapse. Binds to phosphatidylinositol 4,5-bisphosphate.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 35: / Line 35: @@
 __TOC__
 </StructureSection>
-[[Category: Lk3 transgenic mice]]
+[[Category: Large Structures]]
-[[Category: Adams, M E]]
+[[Category: Mus musculus]]
-[[Category: Froehner, S C]]
+[[Category: Adams ME]]
-[[Category: Long, J F]]
+[[Category: Froehner SC]]
-[[Category: Wen, W]]
+[[Category: Long JF]]
-[[Category: Xu, W]]
+[[Category: Wen W]]
-[[Category: Yan, J]]
+[[Category: Xu W]]
-[[Category: Zhang, M]]
+[[Category: Yan J]]
-[[Category: Protein binding]]
+[[Category: Zhang M]]

2adz

From Proteopedia

Current revision

solution structure of the joined PH domain of alpha1-syntrophin

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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