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1q56
From Proteopedia
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'''NMR structure of the B0 isoform of the agrin G3 domain in its Ca2+ bound state''' | '''NMR structure of the B0 isoform of the agrin G3 domain in its Ca2+ bound state''' | ||
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[[Category: Schulthess, T.]] | [[Category: Schulthess, T.]] | ||
[[Category: Stetefeld, J.]] | [[Category: Stetefeld, J.]] | ||
| - | [[Category: | + | [[Category: Achr aggregation]] |
| - | [[Category: | + | [[Category: Ca2+ regulation]] |
| - | [[Category: | + | [[Category: Conformational flexibility]] |
| - | [[Category: | + | [[Category: Laminin-g like domain]] |
| - | [[Category: | + | [[Category: Mrna splicing]] |
| - | [[Category: | + | [[Category: Musk activation]] |
| - | [[Category: | + | [[Category: Nmj synapse]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:52:43 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 02:52, 3 May 2008
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 Page seeded by OCA on Sat May 3 05:52:43 2008
Categories: Gallus gallus | Single protein | Alexandrescu, A T. | Frank, S. | Jenny, M. | Kammerer, R A. | Landwehr, R. | Maciejewski, M W. | Rathgeb-Szabo, K. | Ruegg, M A. | Schulthess, T. | Stetefeld, J. | Achr aggregation | Ca2+ regulation | Conformational flexibility | Laminin-g like domain | Mrna splicing | Musk activation | Nmj synapse
