Group:MUZIC:CapZ
From Proteopedia
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<references/>[http://www.pdb.org/pdb/explore/explore.do?structureId=1IZN] | <references/>[http://www.pdb.org/pdb/explore/explore.do?structureId=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' /> | ||
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| + | {{ABSTRACT_PUBMED_12660160}} | ||
== Structure == | == Structure == | ||
Cap Z was shown to be a stable heterodimer with α and β subunits of 286 and 277 residues, respectively. It is a mixed α-helix and β-sheet protein. CapZ has an elongated structure, with overall dimensions of~90 x 50 x55 Å. The capZ dimer has a pseudo two-fold symmetry, with the monomers joining together to form a central 10-stranded antiparallel <scene name='User:Mara_Camelia_Rusu/Workbench/CapZ/Central_b_sheet/1'>a central 10-stranded β-sheet</scene>. This creates an elongated molecule with the N- and C-terminus of each monomer on opposite faces of the central β -sheet. The C-termini of the subdomains are at opposite ends of the elongated molecule. | Cap Z was shown to be a stable heterodimer with α and β subunits of 286 and 277 residues, respectively. It is a mixed α-helix and β-sheet protein. CapZ has an elongated structure, with overall dimensions of~90 x 50 x55 Å. The capZ dimer has a pseudo two-fold symmetry, with the monomers joining together to form a central 10-stranded antiparallel <scene name='User:Mara_Camelia_Rusu/Workbench/CapZ/Central_b_sheet/1'>a central 10-stranded β-sheet</scene>. This creates an elongated molecule with the N- and C-terminus of each monomer on opposite faces of the central β -sheet. The C-termini of the subdomains are at opposite ends of the elongated molecule. | ||
Revision as of 14:51, 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). [1]
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Template:ABSTRACT PUBMED 12660160
Structure
Cap Z was shown to be a stable heterodimer with α and β subunits of 286 and 277 residues, respectively. It is a mixed α-helix and β-sheet protein. CapZ has an elongated structure, with overall dimensions of~90 x 50 x55 Å. The capZ dimer has a pseudo two-fold symmetry, with the monomers joining together to form a central 10-stranded antiparallel . This creates an elongated molecule with the N- and C-terminus of each monomer on opposite faces of the central β -sheet. The C-termini of the subdomains are at opposite ends of the elongated molecule.
