Plectin: Difference between revisions

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<Structure load='1sh6' size='400' frame='true' align='right' caption='Mouse plectin actin-binding domain' scene='Mouse  plectin actin-binding domain [[1sh6]]'><!--  
<Structure load='1sh6' size='400' frame='true' align='right' caption='Mouse plectin actin-binding domain [[1sh6]]' scene= '><!--  
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Revision as of 13:10, 12 November 2012

<Structure load='1sh6' size='400' frame='true' align='right' caption='Mouse plectin actin-binding domain 1sh6' scene= '>

Plectin, a universal and functionally versatile cytolinker protein, can be divided in three main sections; a central coiled-coil rod domain, N and C-terminal globular region and exhibits a dumbbell like structure [1]. C-terminal region is composed of 6 homologous repeating domains, and this region has a role in binding to intermediate filaments such as vimentin and cytokeratin (2). N-terminal globular region contains actin binding domain (ABD) comprising two calponin homology (CH) domains and N-terminal arm, which varies among isoforms (3). For more details see Group:MUZIC:Plectin.

3D structures of plectin3D structures of plectin

1mb8 – hPCN actin-binding domain – human
1sh5, 1sh6 - PCN actin-binding domain – mouse
3pdy, 3pe0 - hPCN plakin domain
2odu, 2odv – hPCN plakin domain (mutant)
3f7p - hPCN actin-binding domain + integrin β4 residues 1126-1370


  1. Foisner R, Wiche G. Structure and hydrodynamic properties of plectin molecules. J Mol Biol. 1987 Dec 5;198(3):515-31. PMID:3430617

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Jae-Geun Song, Michal Harel, Alexander Berchansky