1u2c
From Proteopedia
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|GENE= | |GENE= | ||
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| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1u2c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u2c OCA], [http://www.ebi.ac.uk/pdbsum/1u2c PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1u2c RCSB]</span> | ||
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[[Category: s6 like fold]] | [[Category: s6 like fold]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:04:25 2008'' |
Revision as of 21:04, 30 March 2008
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| , resolution 2.30Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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
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