1z86

From Proteopedia

(Difference between revisions)

Current revision

Solution structure of the PDZ domain of alpha-syntrophin

Structural highlights

1z86 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/1z86"

@@ Line 1: / Line 1: @@
 ==Solution structure of the PDZ domain of alpha-syntrophin==
-<StructureSection load='1z86' size='340' side='right' caption='[[1z86]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='1z86' size='340' side='right'caption='[[1z86]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1z86]] 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=1Z86 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Z86 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1z86]] 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=1Z86 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Z86 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=1z86 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z86 OCA], [http://pdbe.org/1z86 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1z86 RCSB], [http://www.ebi.ac.uk/pdbsum/1z86 PDBsum]</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=1z86 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z86 OCA], [https://pdbe.org/1z86 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1z86 RCSB], [https://www.ebi.ac.uk/pdbsum/1z86 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1z86 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]]
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/z8/1z86_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/z8/1z86_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 27: / Line 28: @@
 </div>
 <div class="pdbe-citations 1z86" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Syntrophin|Syntrophin]]
 == References ==
 <references/>
 __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]]
-[[Category: Six beta strand]]
-[[Category: Two alpha helix]]

1z86

From Proteopedia

Current revision

Solution structure of the PDZ domain of alpha-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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