http://www.cnr.it/ontology/cnr/individuo/prodotto/ID171502
The structure of the N-terminal region of murine skeletal muscle alpha-dystroglycan discloses a modular architecture (Articolo in rivista)
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- Label
- The structure of the N-terminal region of murine skeletal muscle alpha-dystroglycan discloses a modular architecture (Articolo in rivista) (literal)
- Anno
- 2004-01-01T00:00:00+01:00 (literal)
- Alternative label
Bozic D., Sciandra F., Lamba D., Brancaccio A. (2004)
The structure of the N-terminal region of murine skeletal muscle alpha-dystroglycan discloses a modular architecture
in The Journal of biological chemistry (Print)
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- Bozic D., Sciandra F., Lamba D., Brancaccio A. (literal)
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- ISI Web of Science (WOS) (literal)
- Scopu (literal)
- PubMe (literal)
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- Bozic D. -Biochemisches Institut der Universität Zürich
Sciandra F. -ICRM-CNR, Roma
Lamba D. -IC-CNR, Trieste
Brancaccio A. -ICRM-CNR, Roma (literal)
- Titolo
- The structure of the N-terminal region of murine skeletal muscle alpha-dystroglycan discloses a modular architecture (literal)
- Abstract
- 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-Å 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. (literal)
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