Group:MUZIC:CapZ
From Proteopedia
(Difference between revisions)
(New page: CapZ (Actin Capping Protein) CapZ is expressed in all eukaryotic cells. It binds tightly to the fast growing barbed ends of actin filaments and blocks G-actin association and disassociati...) |
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CapZ is expressed in all eukaryotic cells. It binds tightly 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 tightly 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. | The crystal structure of the sarcomeric form has been resolved to a resolution of 2.1 Å. | ||
Revision as of 13:27, 23 June 2011
== CapZ (Actin Capping Protein)
==
CapZ is expressed in all eukaryotic cells. It binds tightly 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.
