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 Cited by 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: 15016366DOI: 10.1016/j.str.2004.02.001 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.35 Å) |
Structure validation
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