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Group:MUZIC:Myopalladin
From Proteopedia
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<StructureSection load='2dm2' size='500' side='right' caption='NMR structure of the domain Ig1 of human Palladin' | <StructureSection load='2dm2' size='500' side='right' caption='NMR structure of the domain Ig1 of human Palladin' | ||
>Myopalladin (UniProt ID: Q86TC9 [http://www.uniprot.org/uniprot/Q86TC9]) is a protein specific of striated muscles that was identified in a yeast two hybrid screen where the SH3 domain of Nebulin (UniProt ID: P20929 [http://www.uniprot.org/uniprot/P20929],[http://www.proteopedia.org/wiki/index.php/User:Marie-Cecile_Pelissier/Workbench/Nebulin]) was used as a bait. <ref name="Bang">PMID 11309420</ref> It belongs to the family of Actin-Associated Scaffolds, which includes Myotilin, Palladin (UniProt ID: Q8WX93 [http://www.uniprot.org/uniprot/Q8WX93]), and Myopalladin, all three being binding partners of alpha-Actinin. | >Myopalladin (UniProt ID: Q86TC9 [http://www.uniprot.org/uniprot/Q86TC9]) is a protein specific of striated muscles that was identified in a yeast two hybrid screen where the SH3 domain of Nebulin (UniProt ID: P20929 [http://www.uniprot.org/uniprot/P20929],[http://www.proteopedia.org/wiki/index.php/User:Marie-Cecile_Pelissier/Workbench/Nebulin]) was used as a bait. <ref name="Bang">PMID 11309420</ref> It belongs to the family of Actin-Associated Scaffolds, which includes Myotilin, Palladin (UniProt ID: Q8WX93 [http://www.uniprot.org/uniprot/Q8WX93]), and Myopalladin, all three being binding partners of alpha-Actinin. | ||
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==Function and related diseases== | ==Function and related diseases== | ||
Revision as of 13:02, 13 July 2011
Contents |
Introduction
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Domains and Interactions
Ig domains and their binding partners
Myopalladin comprises 5 Ig domains separated by inserted sequences for which no structural domains could be predicted from the sequence. The only structural data related to Myopalladin are the NMR structures of Ig domain 1 (PDB code 2DM2 [[1]]) and Ig domain 2 (PDB code 2DM3 [[2]]) of Palladin (homologous to Ig domains 3 and 4 of Myopalladin, respectively).
CARP
The N-terminal region of Myopalaldin, going from the N-terminal end to the domain Ig2, was shown to interact with the full length CARP. [1]
Alpha-Actinin
The C-terminal region of Myopalaldin, going from the domain Ig3 to the very C-terminal end, was shown to interact with the EF-hand region of Alpha-Actinin. [1]
Inserted sequences and their binding partners
Myopalladin Ig domains are separated by 6 Inserted Sequences (IS). The IS3 comprises a Proline-rich region that has been shown to interact with the SH3 domain of Nebulin and Nebulette. [1]
References
- ↑ 1.0 1.1 1.2 1.3 Bang ML, Mudry RE, McElhinny AS, Trombitas K, Geach AJ, Yamasaki R, Sorimachi H, Granzier H, Gregorio CC, Labeit S. Myopalladin, a novel 145-kilodalton sarcomeric protein with multiple roles in Z-disc and I-band protein assemblies. J Cell Biol. 2001 Apr 16;153(2):413-27. PMID:11309420
- ↑ Duboscq-Bidot L, Xu P, Charron P, Neyroud N, Dilanian G, Millaire A, Bors V, Komajda M, Villard E. Mutations in the Z-band protein myopalladin gene and idiopathic dilated cardiomyopathy. Cardiovasc Res. 2008 Jan;77(1):118-25. Epub 2007 Sep 19. PMID:18006477 doi:10.1093/cvr/cvm015
