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[[Image:2adz.gif|left|200px]]
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{{STRUCTURE_2adz|  PDB=2adz  |  SCENE=  }}
'''solution structure of the joined PH domain of alpha1-syntrophin'''


==solution structure of the joined PH domain of alpha1-syntrophin==
<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 [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='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'>[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 ==
[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/ad/2adz_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2adz ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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.


==Overview==
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<ref>PMID:16252003</ref>
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.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
2ADZ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ADZ OCA].
</div>
<div class="pdbe-citations 2adz" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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:[http://www.ncbi.nlm.nih.gov/pubmed/16252003 16252003]
*[[Syntrophin|Syntrophin]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Adams ME]]
[[Category: Adams, M E.]]
[[Category: Froehner SC]]
[[Category: Froehner, S C.]]
[[Category: Long JF]]
[[Category: Long, J F.]]
[[Category: Wen W]]
[[Category: Wen, W.]]
[[Category: Xu W]]
[[Category: Xu, W.]]
[[Category: Yan J]]
[[Category: Yan, J.]]
[[Category: Zhang M]]
[[Category: Zhang, M.]]
[[Category: Protein binding]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 18:55:31 2008''
Retrieved from "https://proteopedia.org/2adz"