1q56 | pdb_00001q56

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

File:1q56.jpg

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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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