1u2c

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(New page: 200px<br /><applet load="1u2c" size="450" color="white" frame="true" align="right" spinBox="true" caption="1u2c, resolution 2.30&Aring;" /> '''Crystal Structure of...)
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[[Image:1u2c.jpg|left|200px]]<br /><applet load="1u2c" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1u2c.jpg|left|200px]]<br /><applet load="1u2c" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1u2c, resolution 2.30&Aring;" />
caption="1u2c, resolution 2.30&Aring;" />
'''Crystal Structure of a-dystroglycan'''<br />
'''Crystal Structure of a-dystroglycan'''<br />
==Overview==
==Overview==
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Dystroglycan (DG) is a cell surface receptor consisting of two subunits:, alpha-dystroglycan, extracellular and highly glycosylated, and, beta-dystroglycan, spanning the cell membrane. It is a pivotal member of, the dystrophin-glycoprotein complex and is involved in a wide variety of, important cellular processes such as the stabilization of the muscle fiber, sarcolemma or the clustering of acetylcholine receptors. We report the, 2.3-A resolution crystal structure of the murine skeletal muscle, N-terminal alpha-DG region, which confirms the presence of two autonomous, domains; the first finally identified as an Ig-like and the second, resembling ribosomal RNA-binding proteins. Solid-phase laminin binding, assays show the occurrence of protein-protein type of interactions, involving the Ig-like domain of alpha-DG.
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Dystroglycan (DG) is a cell surface receptor consisting of two subunits: alpha-dystroglycan, extracellular and highly glycosylated, and beta-dystroglycan, spanning the cell membrane. It is a pivotal member of the dystrophin-glycoprotein complex and is involved in a wide variety of important cellular processes such as the stabilization of the muscle fiber sarcolemma or the clustering of acetylcholine receptors. We report the 2.3-A resolution crystal structure of the murine skeletal muscle N-terminal alpha-DG region, which confirms the presence of two autonomous domains; the first finally identified as an Ig-like and the second resembling ribosomal RNA-binding proteins. Solid-phase laminin binding assays show the occurrence of protein-protein type of interactions involving the Ig-like domain of alpha-DG.
==About this Structure==
==About this Structure==
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1U2C is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1U2C OCA].
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1U2C is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U2C OCA].
==Reference==
==Reference==
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[[Category: s6 like fold]]
[[Category: s6 like fold]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:47:38 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:19:52 2008''

Revision as of 13:19, 21 February 2008


1u2c, resolution 2.30Å

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Crystal Structure of a-dystroglycan

Overview

Dystroglycan (DG) is a cell surface receptor consisting of two subunits: alpha-dystroglycan, extracellular and highly glycosylated, and beta-dystroglycan, spanning the cell membrane. It is a pivotal member of the dystrophin-glycoprotein complex and is involved in a wide variety of important cellular processes such as the stabilization of the muscle fiber sarcolemma or the clustering of acetylcholine receptors. We report the 2.3-A resolution crystal structure of the murine skeletal muscle N-terminal alpha-DG region, which confirms the presence of two autonomous domains; the first finally identified as an Ig-like and the second resembling ribosomal RNA-binding proteins. Solid-phase laminin binding assays show the occurrence of protein-protein type of interactions involving the Ig-like domain of alpha-DG.

About this Structure

1U2C is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

The structure of the N-terminal region of murine skeletal muscle alpha-dystroglycan discloses a modular architecture., Bozic D, Sciandra F, Lamba D, Brancaccio A, J Biol Chem. 2004 Oct 22;279(43):44812-6. Epub 2004 Aug 23. PMID:15326183

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