1u2c
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1u2c.jpg|left|200px]] | + | [[Image:1u2c.jpg|left|200px]] |
| - | + | ||
| - | '''Crystal Structure of a-dystroglycan''' | + | {{Structure |
| + | |PDB= 1u2c |SIZE=350|CAPTION= <scene name='initialview01'>1u2c</scene>, resolution 2.30Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Crystal Structure of a-dystroglycan''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1U2C is a [ | + | 1U2C is a [[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== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15326183 15326183] |
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 20: | Line 29: | ||
[[Category: s6 like fold]] | [[Category: s6 like fold]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:26:23 2008'' |
Revision as of 12:26, 20 March 2008
| |||||||
| , resolution 2.30Å | |||||||
|---|---|---|---|---|---|---|---|
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
Page seeded by OCA on Thu Mar 20 14:26:23 2008
