Group:MUZIC:CapZ
From Proteopedia
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== CapZ (Actin Capping Protein) == | == CapZ (Actin Capping Protein) == | ||
| - | CapZ is expressed in all eukaryotic cells. It binds | + | 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 α 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 α 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). | ||
<Structure load='1IZN' size='500' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /> | <Structure load='1IZN' size='500' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /> | ||
Revision as of 13:42, 23 June 2011
CapZ (Actin Capping Protein)
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 α 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).
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