1u2c is a 1 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
[DAG1_MOUSE] The dystroglycan complex is involved in a number of processes including laminin and basement membrane assembly, sacrolemmal stability, cell survival, peripheral nerve myelination, nodal structure, cell migration, and epithelial polarization.[1][2][3] Alpha-dystroglycan is an extracellular peripheral glycoprotein that acts as a receptor for both extracellular matrix proteins containing laminin-G domains, and for certain adenoviruses. Receptor for laminin-2 (LAMA2) and agrin in peripheral nerve Schwann cells. Also receptor for lymphocytic choriomeningitis virus, Old World Lassa fever virus, and clade C New World arenaviruses.[4][5][6] Beta-dystroglycan is a transmembrane protein that plays important roles in connecting the extracellular matrix to the cytoskeleton. Acts as a cell adhesion receptor in both muscle and non-muscle tissues. Receptor for both DMD and UTRN and, through these interactions, scaffolds axin to the cytoskeleton. Also functions in cell adhesion-mediated signaling and implicated in cell polarity (By similarity).[7][8][9]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[10]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑Williamson RA, Henry MD, Daniels KJ, Hrstka RF, Lee JC, Sunada Y, Ibraghimov-Beskrovnaya O, Campbell KP. Dystroglycan is essential for early embryonic development: disruption of Reichert's membrane in Dag1-null mice. Hum Mol Genet. 1997 Jun;6(6):831-41. PMID:9175728
↑Previtali SC, Nodari A, Taveggia C, Pardini C, Dina G, Villa A, Wrabetz L, Quattrini A, Feltri ML. Expression of laminin receptors in schwann cell differentiation: evidence for distinct roles. J Neurosci. 2003 Jul 2;23(13):5520-30. PMID:12843252
↑Saito F, Moore SA, Barresi R, Henry MD, Messing A, Ross-Barta SE, Cohn RD, Williamson RA, Sluka KA, Sherman DL, Brophy PJ, Schmelzer JD, Low PA, Wrabetz L, Feltri ML, Campbell KP. Unique role of dystroglycan in peripheral nerve myelination, nodal structure, and sodium channel stabilization. Neuron. 2003 Jun 5;38(5):747-58. PMID:12797959
↑Williamson RA, Henry MD, Daniels KJ, Hrstka RF, Lee JC, Sunada Y, Ibraghimov-Beskrovnaya O, Campbell KP. Dystroglycan is essential for early embryonic development: disruption of Reichert's membrane in Dag1-null mice. Hum Mol Genet. 1997 Jun;6(6):831-41. PMID:9175728
↑Previtali SC, Nodari A, Taveggia C, Pardini C, Dina G, Villa A, Wrabetz L, Quattrini A, Feltri ML. Expression of laminin receptors in schwann cell differentiation: evidence for distinct roles. J Neurosci. 2003 Jul 2;23(13):5520-30. PMID:12843252
↑Saito F, Moore SA, Barresi R, Henry MD, Messing A, Ross-Barta SE, Cohn RD, Williamson RA, Sluka KA, Sherman DL, Brophy PJ, Schmelzer JD, Low PA, Wrabetz L, Feltri ML, Campbell KP. Unique role of dystroglycan in peripheral nerve myelination, nodal structure, and sodium channel stabilization. Neuron. 2003 Jun 5;38(5):747-58. PMID:12797959
↑Williamson RA, Henry MD, Daniels KJ, Hrstka RF, Lee JC, Sunada Y, Ibraghimov-Beskrovnaya O, Campbell KP. Dystroglycan is essential for early embryonic development: disruption of Reichert's membrane in Dag1-null mice. Hum Mol Genet. 1997 Jun;6(6):831-41. PMID:9175728
↑Previtali SC, Nodari A, Taveggia C, Pardini C, Dina G, Villa A, Wrabetz L, Quattrini A, Feltri ML. Expression of laminin receptors in schwann cell differentiation: evidence for distinct roles. J Neurosci. 2003 Jul 2;23(13):5520-30. PMID:12843252
↑Saito F, Moore SA, Barresi R, Henry MD, Messing A, Ross-Barta SE, Cohn RD, Williamson RA, Sluka KA, Sherman DL, Brophy PJ, Schmelzer JD, Low PA, Wrabetz L, Feltri ML, Campbell KP. Unique role of dystroglycan in peripheral nerve myelination, nodal structure, and sodium channel stabilization. Neuron. 2003 Jun 5;38(5):747-58. PMID:12797959
↑Bozic D, Sciandra F, Lamba D, Brancaccio A. The structure of the N-terminal region of murine skeletal muscle alpha-dystroglycan discloses a modular architecture. J Biol Chem. 2004 Oct 22;279(43):44812-6. Epub 2004 Aug 23. PMID:15326183 doi:10.1074/jbc.C400353200
