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1q56
From Proteopedia
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| - | [[Image:1q56.jpg|left|200px]] | + | [[Image:1q56.jpg|left|200px]] |
| - | + | ||
| - | '''NMR structure of the B0 isoform of the agrin G3 domain in its Ca2+ bound state''' | + | {{Structure |
| + | |PDB= 1q56 |SIZE=350|CAPTION= <scene name='initialview01'>1q56</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= AGRN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9031 Gallus gallus]) | ||
| + | }} | ||
| + | |||
| + | '''NMR structure of the B0 isoform of the agrin G3 domain in its Ca2+ bound state''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1Q56 is a [ | + | 1Q56 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q56 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15016366 15016366] |
[[Category: Gallus gallus]] | [[Category: Gallus gallus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: nmj synapse]] | [[Category: nmj synapse]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:33:05 2008'' |
Revision as of 11:33, 20 March 2008
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| Gene: | AGRN (Gallus gallus) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Thu Mar 20 13:33:05 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
