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==Solution structure of the N-terminal LIM domain of MLP/CRP3== | ==Solution structure of the N-terminal LIM domain of MLP/CRP3== | ||
<StructureSection load='2o10' size='340' side='right'caption='[[2o10 | <StructureSection load='2o10' size='340' side='right'caption='[[2o10]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2o10]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2o10]] 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=2O10 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2O10 FirstGlance]. <br> | ||
</td></tr><tr id=' | </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=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=2o10 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o10 OCA], [https://pdbe.org/2o10 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2o10 RCSB], [https://www.ebi.ac.uk/pdbsum/2o10 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2o10 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=2o10 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o10 OCA], [https://pdbe.org/2o10 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2o10 RCSB], [https://www.ebi.ac.uk/pdbsum/2o10 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2o10 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Disease == | == Disease == | ||
[https://www.uniprot.org/uniprot/CSRP3_HUMAN CSRP3_HUMAN] Defects in CSRP3 are the cause of cardiomyopathy dilated type 1M (CMD1M) [MIM:[https://omim.org/entry/607482 607482]. 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:18505755</ref> <ref>PMID:12507422</ref> Defects in CSRP3 are the cause of familial hypertrophic cardiomyopathy type 12 (CMH12) [MIM:[https://omim.org/entry/612124 612124]. Familial hypertrophic cardiomyopathy is a hereditary heart disorder characterized by ventricular hypertrophy, which is usually asymmetric and often involves the interventricular septum. The symptoms include dyspnea, syncope, collapse, palpitations, and chest pain. They can be readily provoked by exercise. The disorder has inter- and intrafamilial variability ranging from benign to malignant forms with high risk of cardiac failure and sudden cardiac death.<ref>PMID:18505755</ref> <ref>PMID:12642359</ref> | |||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/CSRP3_HUMAN CSRP3_HUMAN] Positive regulator of myogenesis. Plays a crucial and specific role in the organization of cytosolic structures in cardiomyocytes. Could play a role in mechanical stretch sensing. May be a scaffold protein that promotes the assembly of interacting proteins at Z-line structures. It is essential for calcineurin anchorage to the Z line. Required for stress-induced calcineurin-NFAT activation (By similarity). | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Edlich | [[Category: Edlich C]] | ||
[[Category: Muhle-Goll | [[Category: Muhle-Goll C]] | ||
[[Category: Schallus | [[Category: Schallus T]] | ||
Latest revision as of 03:12, 28 December 2023
Solution structure of the N-terminal LIM domain of MLP/CRP3Solution structure of the N-terminal LIM domain of MLP/CRP3
Structural highlights
DiseaseCSRP3_HUMAN Defects in CSRP3 are the cause of cardiomyopathy dilated type 1M (CMD1M) [MIM:607482. 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 CSRP3 are the cause of familial hypertrophic cardiomyopathy type 12 (CMH12) [MIM:612124. Familial hypertrophic cardiomyopathy is a hereditary heart disorder characterized by ventricular hypertrophy, which is usually asymmetric and often involves the interventricular septum. The symptoms include dyspnea, syncope, collapse, palpitations, and chest pain. They can be readily provoked by exercise. The disorder has inter- and intrafamilial variability ranging from benign to malignant forms with high risk of cardiac failure and sudden cardiac death.[3] [4] FunctionCSRP3_HUMAN Positive regulator of myogenesis. Plays a crucial and specific role in the organization of cytosolic structures in cardiomyocytes. Could play a role in mechanical stretch sensing. May be a scaffold protein that promotes the assembly of interacting proteins at Z-line structures. It is essential for calcineurin anchorage to the Z line. Required for stress-induced calcineurin-NFAT activation (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See AlsoReferences
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