Modulation of agrin function by alternative splicing and Ca2+ binding

Stetefeld, J. and Alexandrescu, A. T. and Maciejewski, M. W. and Jenny, M. and Rathgeb-Szabo, K. and Schulthess, T. and Landwehr, R. and Frank, S. and Ruegg, M. A. and Kammerer, R. A.. (2004) Modulation of agrin function by alternative splicing and Ca2+ binding. Structure: with folding and design, Vol. 12, H. 3. pp. 503-515.

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The aggregation of acetylcholine receptors on postsynaptic membranes is a key step in neuromuscular junction development. This process depends on alternatively spliced forms of the proteoglycan agrin with "B-inserts" of 8, 11, or 19 residues in the protein's globular C-terminal domain, G3. Structures of the neural B8 and B11 forms of agrin-G3 were determined by X-ray crystallography. The structure of G3-B0, which lacks inserts, was determined by NMR. The agrin-G3 domain adopts a beta jellyroll fold. The B insert site is flanked by four loops on one edge of the beta sandwich. The loops form a surface that corresponds to a versatile interaction interface in the family of structurally related LNS proteins. NMR and X-ray data indicate that this interaction interface is flexible in agrin-G3 and that flexibility is reduced by Ca(2+) binding. The plasticity of the interaction interface could enable different splice forms of agrin to select between multiple binding partners.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Neurobiology > Pharmacology/Neurobiology (Rüegg)
UniBasel Contributors:Rüegg, Markus A.
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:Current Biology
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:16 Apr 2019 12:59
Deposited On:22 Mar 2012 13:31

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