Group:MUZIC:Plectin
From Proteopedia
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<Structure load='1sh5' size='500' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /> | <Structure load='1sh5' size='500' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /> | ||
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| + | <Structure load='1sh6' size='500' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />== Overall structure == | ||
Plectin 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. 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 <ref>PMID:3430617</ref>. N-terminal globular region contains actin binding domain (ABD) comprising two calponin homology (CH) domains and N-terminal arm, which varies among isoforms<ref>PMID:10556294</ref>. | Plectin 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. 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 <ref>PMID:3430617</ref>. N-terminal globular region contains actin binding domain (ABD) comprising two calponin homology (CH) domains and N-terminal arm, which varies among isoforms<ref>PMID:10556294</ref>. | ||
<references/> | <references/> | ||
Revision as of 07:38, 24 June 2011
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Plectin 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. 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 [1]. N-terminal globular region contains actin binding domain (ABD) comprising two calponin homology (CH) domains and N-terminal arm, which varies among isoforms[2].
- ↑ Foisner R, Wiche G. Structure and hydrodynamic properties of plectin molecules. J Mol Biol. 1987 Dec 5;198(3):515-31. PMID:3430617
- ↑ Fuchs P, Zorer M, Rezniczek GA, Spazierer D, Oehler S, Castanon MJ, Hauptmann R, Wiche G. Unusual 5' transcript complexity of plectin isoforms: novel tissue-specific exons modulate actin binding activity. Hum Mol Genet. 1999 Dec;8(13):2461-72. PMID:10556294
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