1q56

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NMR structure of the B0 isoform of the agrin G3 domain in its Ca2+ bound state

Overview

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.

About this Structure

1Q56 is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.

Reference

Modulation of agrin function by alternative splicing and Ca2+ binding., Stetefeld J, Alexandrescu AT, Maciejewski MW, Jenny M, Rathgeb-Szabo K, Schulthess T, Landwehr R, Frank S, Ruegg MA, Kammerer RA, Structure. 2004 Mar;12(3):503-15. PMID:15016366

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