Plectin
From Proteopedia
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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/><!-- | + | <Structure load='1sh6' size='400' frame='true' align='right' caption='Mouse plectin actin-binding domain' scene='Mouse plectin actin-binding domain [[1sh6]]/><!-- |
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Revision as of 10:44, 13 August 2012
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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 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
- ↑ Foisner R, Wiche G. Structure and hydrodynamic properties of plectin molecules. J Mol Biol. 1987 Dec 5;198(3):515-31. PMID:3430617
