View source for 1rgw


==Solution Structure of ZASP's PDZ domain==
<StructureSection load='1rgw' size='340' side='right'caption='[[1rgw]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1rgw]] 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=1RGW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RGW 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=1rgw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rgw OCA], [https://pdbe.org/1rgw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rgw RCSB], [https://www.ebi.ac.uk/pdbsum/1rgw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rgw ProSAT]</span></td></tr>
</table>
== Disease ==
[https://www.uniprot.org/uniprot/LDB3_HUMAN LDB3_HUMAN] Defects in LDB3 are the cause of cardiomyopathy dilated type 1C (CMD1C) [MIM:[https://omim.org/entry/601493 601493]. Dilated cardiomyopathy is a disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death.<ref>PMID:14662268</ref> <ref>PMID:14660611</ref>   Defects in LDB3 are the cause of left ventricular non-compaction type 3 (LVNC3) [MIM:[https://omim.org/entry/601493 601493]. Left ventricular non-compaction is characterized by numerous prominent trabeculations and deep intertrabecular recesses in hypertrophied and hypokinetic segments of the left ventricle.  Defects in LDB3 are the cause of myopathy myofibrillar type 4 (MFM4) [MIM:[https://omim.org/entry/609452 609452]. A neuromuscular disorder characterized by distal and proximal muscle weakness with signs of cardiomyopathy and neuropathy.
== Function ==
[https://www.uniprot.org/uniprot/LDB3_HUMAN LDB3_HUMAN] May function as an adapter in striated muscle to couple protein kinase C-mediated signaling via its LIM domains to the cytoskeleton.[:]
== 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/rg/1rgw_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=1rgw ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Z band alternately spliced PDZ-containing protein (ZASP) is a sarcomere Z disk protein expressed in human cardiac and skeletal muscle that is thought to be involved in a dominant familial dilated cardiomyopathy. The N-terminal PDZ domain of ZASP interacts with the C terminus of alpha-actinin-2, the major component of the Z disk, probably by forming a ternary complex with titin Z repeats. We have determined the structure of ZASP PDZ by NMR and showed that it is a classical class 1 PDZ domain that recognizes the carboxy-terminal sequence of an alpha-actinin-2 calmodulin-like domain with micromolar affinity. We also characterized the role of each component in the ternary complex ZASP/alpha-actinin-2/titin, showing that the alpha-actinin-2/ZASP PDZ interaction involves a binding surface distinct from that recognized by the titin Z repeats. ZASP PDZ structure was used to model other members of the enigma family by homology and to predict their abilities to bind alpha-actinin-2.

Solution structure of ZASP PDZ domain; implications for sarcomere ultrastructure and enigma family redundancy.,Au Y, Atkinson RA, Guerrini R, Kelly G, Joseph C, Martin SR, Muskett FW, Pallavicini A, Faulkner G, Pastore A Structure. 2004 Apr;12(4):611-22. PMID:15062084<ref>PMID:15062084</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1rgw" style="background-color:#fffaf0;"></div>

==See Also==
*[[PDZ and LIM domain protein|PDZ and LIM domain protein]]
*[[ZASP protein|ZASP protein]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Atkinson RA]]
[[Category: Au Y]]
[[Category: Faulkner G]]
[[Category: Guerrini R]]
[[Category: Joseph C]]
[[Category: Martin SR]]
[[Category: Muskett FW]]
[[Category: Pallavicini A]]
[[Category: Pastore A]]