Group:MUZIC:CapZ: Difference between revisions
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== CapZ (Actin Capping Protein, CP) == | == CapZ (Actin Capping Protein, CP) == | ||
[[Image:1izn_bio_r_500.jpg]] | [[Image:1izn_bio_r_500.jpg]] CapZ is expressed in all eukaryotic cells. It binds to the fast growing barbed ends of actin filaments and blocks G-actin association and disassociation, thus regulating actin filament dynamics. In skeletal muscle it localizes at the Z-disk. | ||
CapZ is expressed in all eukaryotic cells. It binds to the fast growing barbed ends of actin filaments and blocks G-actin association and disassociation, thus regulating actin filament dynamics. In skeletal muscle it localizes at the Z-disk. | |||
Cap Z is a heterodimer composed of two subunits <scene name='User:Mara_Camelia_Rusu/Workbench/CapZ/Alpha_subunit/1'>α</scene> and β and there are at least two isoforms of each of the subunits. In cardiomyocites the β1 containing isoform localizes to the Z-disk and β2 containing isoform localizes to the cell periphery and intercalated disc. | Cap Z is a heterodimer composed of two subunits <scene name='User:Mara_Camelia_Rusu/Workbench/CapZ/Alpha_subunit/1'>α</scene> and β and there are at least two isoforms of each of the subunits. In cardiomyocites the β1 containing isoform localizes to the Z-disk and β2 containing isoform localizes to the cell periphery and intercalated disc. | ||
The crystal structure of the sarcomeric form has been resolved to a resolution of 2.1 Å by X-ray crystallography (1IZN). | The crystal structure of the sarcomeric form has been resolved to a resolution of 2.1 Å by X-ray crystallography (1IZN). | ||