1u2c: Difference between revisions

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[[Image:1u2c.jpg|left|200px]]<br /><applet load="1u2c" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1u2c.jpg|left|200px]]<br /><applet load="1u2c" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1u2c, resolution 2.30Å" />

'''Crystal Structure of a-dystroglycan'''<br />

==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.

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 [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].

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==

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[[Category: s6 like fold]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Wed Nov~~ 21 03:47:~~38 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:19:52 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1u2c.jpg|left|200px]]<br /><applet load="1u2c" size="450" color="white" frame="true" align="right" spinBox="true"
+[[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;" />
 '''Crystal Structure of a-dystroglycan'''<br />
 ==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.
+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==
-U2C 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].
+U2C 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==
@@ Line 20: / Line 20: @@
 [[Category: s6 like fold]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:47:38 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:19:52 2008''