1PZ8

Modulation of agrin function by alternative splicing and Ca2+ binding

Summary for 1PZ8

• Entry DOI: 10.2210/pdb1pz8/pdb
• Related: 1PZ7 1Q56
• Descriptor: Agrin, CALCIUM ION (3 entities in total)
• Functional Keywords: agrin, structural protein
• Biological source: Gallus gallus (chicken)
• Cellular location: Secreted, extracellular space, extracellular matrix: P31696
• Total number of polymer chains: 4
• Total formula weight: 88368.50

Authors

Stetefeld, J.,Alexandrescu, A.T.,Maciejewski, M.W.,Jenny, M.,Rathgeb-Szabo, K.,Schulthess, T.,Landwehr, R.,Frank, S.,Ruegg, M.A.,Kammerer, R.A. (deposition date: 2003-07-10, release date: 2004-04-13, Last modification date: 2024-11-06)

Primary citation

Stetefeld, J.,Alexandrescu, A.T.,Maciejewski, M.W.,Jenny, M.,Rathgeb-Szabo, K.,Schulthess, T.,Landwehr, R.,Frank, S.,Ruegg, M.A.,Kammerer, R.A.
Modulation of agrin function by alternative splicing and Ca2+ binding.
STRUCTURE, 12:503-515, 2004

PubMed Abstract: 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.

PubMed: 15016366
DOI: 10.1016/j.str.2004.02.001

Experimental method

X-RAY DIFFRACTION (2.35 Å)