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==Crystal structure of N-terminal PDZ domain of ZASP in complex with myotilin C-terminal peptide.== | ==Crystal structure of N-terminal PDZ domain of ZASP in complex with myotilin C-terminal peptide.== | ||
<StructureSection load='4ydp' size='340' side='right' caption='[[4ydp]], [[Resolution|resolution]] 1.40Å' scene=''> | <StructureSection load='4ydp' size='340' side='right'caption='[[4ydp]], [[Resolution|resolution]] 1.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4ydp]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YDP OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[4ydp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YDP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YDP FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</scene>, <scene name='pdbligand=LEU:LEUCINE'>LEU</scene></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</scene>, <scene name='pdbligand=LEU:LEUCINE'>LEU</scene></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=4ydp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ydp OCA], [https://pdbe.org/4ydp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ydp RCSB], [https://www.ebi.ac.uk/pdbsum/4ydp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ydp ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Disease == | == 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 == | == 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.[:] | ||
==See Also== | |||
*[[PDZ and LIM domain protein|PDZ and LIM domain protein]] | |||
*[[ZASP protein|ZASP protein]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Djinovic-Carugo K]] | ||
[[Category: | [[Category: Grishkovskaya I]] | ||
[[Category: | [[Category: Kontaxis G]] | ||
[[Category: | [[Category: Onipe A]] | ||
Latest revision as of 13:54, 10 January 2024
Crystal structure of N-terminal PDZ domain of ZASP in complex with myotilin C-terminal peptide.Crystal structure of N-terminal PDZ domain of ZASP in complex with myotilin C-terminal peptide.
Structural highlights
DiseaseLDB3_HUMAN Defects in LDB3 are the cause of cardiomyopathy dilated type 1C (CMD1C) [MIM: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.[1] [2] Defects in LDB3 are the cause of left ventricular non-compaction type 3 (LVNC3) [MIM: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:609452. A neuromuscular disorder characterized by distal and proximal muscle weakness with signs of cardiomyopathy and neuropathy. FunctionLDB3_HUMAN May function as an adapter in striated muscle to couple protein kinase C-mediated signaling via its LIM domains to the cytoskeleton.[:] See AlsoReferences
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