Plectin
<Structure load='1sh6' size='400' 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], [3]. 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
Updated on 05-July-2016
1mb8, 4q59 – hPCN actin-binding domain – human
1sh5, 1sh6 - PCN actin-binding domain – mouse
3pdy, 3pe0 - hPCN plakin domain
2odu, 2odv – hPCN plakin domain (mutant)
4gdo – hPCN rod domain
3f7p, 4q58 - hPCN actin-binding domain + integrin β4 residues 1126-1370
4q57 - hPCN actin-binding domain + calmodulin N terminal
ReferencesReferences
- ↑ Foisner R, Wiche G. Structure and hydrodynamic properties of plectin molecules. J Mol Biol. 1987 Dec 5;198(3):515-31. PMID:3430617
- ↑ Sutoh Yoneyama M, Hatakeyama S, Habuchi T, Inoue T, Nakamura T, Funyu T, Wiche G, Ohyama C, Tsuboi S. Vimentin intermediate filament and plectin provide a scaffold for invadopodia, facilitating cancer cell invasion and extravasation for metastasis. Eur J Cell Biol. 2014 Apr;93(4):157-69. doi: 10.1016/j.ejcb.2014.03.002. Epub, 2014 Apr 15. PMID:24810881 doi:http://dx.doi.org/10.1016/j.ejcb.2014.03.002
- ↑ Bouameur JE, Favre B, Fontao L, Lingasamy P, Begre N, Borradori L. Interaction of plectin with keratins 5 and 14: dependence on several plectin domains and keratin quaternary structure. J Invest Dermatol. 2014 Nov;134(11):2776-83. doi: 10.1038/jid.2014.255. Epub 2014, Jun 18. PMID:24940650 doi:http://dx.doi.org/10.1038/jid.2014.255