1izn

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(New page: 200px<br /><applet load="1izn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1izn, resolution 2.1&Aring;" /> '''Crystal Structure of ...)
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[[Image:1izn.gif|left|200px]]<br /><applet load="1izn" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1izn.gif|left|200px]]<br /><applet load="1izn" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1izn, resolution 2.1&Aring;" />
caption="1izn, resolution 2.1&Aring;" />
'''Crystal Structure of Actin Filament Capping Protein CapZ'''<br />
'''Crystal Structure of Actin Filament Capping Protein CapZ'''<br />
==Overview==
==Overview==
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Capping protein, a heterodimeric protein composed of alpha and beta, subunits, is a key cellular component regulating actin filament assembly, and organization. It binds to the barbed ends of the filaments and works, as a 'cap' by preventing the addition and loss of actin monomers at the, end. Here we describe the crystal structure of the chicken sarcomeric, capping protein CapZ at 2.1 A resolution. The structure shows a striking, resemblance between the alpha and beta subunits, so that the entire, molecule has a pseudo 2-fold rotational symmetry. CapZ has a pair of, mobile extensions for actin binding, one of which also provides, concomitant binding to another protein for the actin filament targeting., The mobile extensions probably form flexible links to the end of the actin, filament with a pseudo 2(1) helical symmetry, enabling the docking of the, two in a symmetry mismatch.
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Capping protein, a heterodimeric protein composed of alpha and beta subunits, is a key cellular component regulating actin filament assembly and organization. It binds to the barbed ends of the filaments and works as a 'cap' by preventing the addition and loss of actin monomers at the end. Here we describe the crystal structure of the chicken sarcomeric capping protein CapZ at 2.1 A resolution. The structure shows a striking resemblance between the alpha and beta subunits, so that the entire molecule has a pseudo 2-fold rotational symmetry. CapZ has a pair of mobile extensions for actin binding, one of which also provides concomitant binding to another protein for the actin filament targeting. The mobile extensions probably form flexible links to the end of the actin filament with a pseudo 2(1) helical symmetry, enabling the docking of the two in a symmetry mismatch.
==About this Structure==
==About this Structure==
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1IZN is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with NO3 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IZN OCA].
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1IZN is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with <scene name='pdbligand=NO3:'>NO3</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IZN OCA].
==Reference==
==Reference==
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[[Category: heterodimer]]
[[Category: heterodimer]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:48:24 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:17:23 2008''

Revision as of 11:17, 21 February 2008


1izn, resolution 2.1Å

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Crystal Structure of Actin Filament Capping Protein CapZ

Overview

Capping protein, a heterodimeric protein composed of alpha and beta subunits, is a key cellular component regulating actin filament assembly and organization. It binds to the barbed ends of the filaments and works as a 'cap' by preventing the addition and loss of actin monomers at the end. Here we describe the crystal structure of the chicken sarcomeric capping protein CapZ at 2.1 A resolution. The structure shows a striking resemblance between the alpha and beta subunits, so that the entire molecule has a pseudo 2-fold rotational symmetry. CapZ has a pair of mobile extensions for actin binding, one of which also provides concomitant binding to another protein for the actin filament targeting. The mobile extensions probably form flexible links to the end of the actin filament with a pseudo 2(1) helical symmetry, enabling the docking of the two in a symmetry mismatch.

About this Structure

1IZN is a Protein complex structure of sequences from Gallus gallus with as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structure of CapZ: structural basis for actin filament barbed end capping., Yamashita A, Maeda K, Maeda Y, EMBO J. 2003 Apr 1;22(7):1529-38. PMID:12660160

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