PDZ and LIM domain protein

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<StructureSection load='2pa1' size='350' side='right' caption='Structure of PDZ and LIM domain protein 2 PDZ domain with C-terminal of β-tropomyosin and Cl- ions (PDB entry [[2pa1]])' scene=''>
<StructureSection load='2pa1' size='350' side='right' caption='Structure of PDZ and LIM domain protein 2 PDZ domain with C-terminal of β-tropomyosin and Cl- ions (PDB entry [[2pa1]])' scene=''>
== Function ==
== Function ==
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'''PDZ and LIM domain proteins''' (PDLIM) contain PDZ and LIM domains. PDLIM binds α-actinin via its PDZ domain and other proteins via its LIM domain. PDLIM is implicated in cardiac and skeletal muscle structure<ref>PMID:17767364</ref>.<br /> For details on PDLIM1 see [[Group:MUZIC:ALP]].<br />For details on PDLIM see [[Group:MUZIC:ZASP]] and [[Group:MUZIC:Enigma Family]].
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'''PDZ and LIM domain proteins''' (PDLIM) contain PDZ and LIM domains. PDLIM binds α-actinin via its PDZ domain and other proteins via its LIM domain. PDLIM is implicated in cardiac and skeletal muscle structure<ref>PMID:17767364</ref>.<br /> For details on PDLIM see [[Group:MUZIC:ZASP]] and [[Group:MUZIC:Enigma Family]].
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*'''PDLIM1''' promotes cell attachment at the cytoskeleton.<br />
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*'''PDLIM1''' promotes cell attachment at the cytoskeleton. For details see [[Group:MUZIC:ALP]].<br />
*'''PDLIM2''' may have a role in bringing proteins to the cytoskeleton.<br />
*'''PDLIM2''' may have a role in bringing proteins to the cytoskeleton.<br />
*'''PDLIM3''' may have a role in organizing actin filament arrays within muscle cells.<br />
*'''PDLIM3''' may have a role in organizing actin filament arrays within muscle cells.<br />

Revision as of 10:24, 15 June 2016

Structure of PDZ and LIM domain protein 2 PDZ domain with C-terminal of β-tropomyosin and Cl- ions (PDB entry 2pa1)

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3D structures of PDZ and LIM domain protein

Updated on 15-June-2016

References

  1. te Velthuis AJ, Bagowski CP. PDZ and LIM domain-encoding genes: molecular interactions and their role in development. ScientificWorldJournal. 2007 Sep 1;7:1470-92. PMID:17767364 doi:10.1100/tsw.2007.232

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