1pz7
From Proteopedia
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- | [[Image:1pz7.jpg|left|200px]] | + | [[Image:1pz7.jpg|left|200px]] |
- | + | ||
- | '''Modulation of agrin function by alternative splicing and Ca2+ binding''' | + | {{Structure |
+ | |PDB= 1pz7 |SIZE=350|CAPTION= <scene name='initialview01'>1pz7</scene>, resolution 1.421Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | ||
+ | |ACTIVITY= | ||
+ | |GENE= AGRN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9031 Gallus gallus]) | ||
+ | }} | ||
+ | |||
+ | '''Modulation of agrin function by alternative splicing and Ca2+ binding''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1PZ7 is a [ | + | 1PZ7 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=1PZ7 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: agrin]] | [[Category: agrin]] | ||
- | ''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 13:30:55 2008'' |
Revision as of 11:30, 20 March 2008
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, resolution 1.421Å | |||||||
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Ligands: | |||||||
Gene: | AGRN (Gallus gallus) | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Modulation of agrin function by alternative splicing and Ca2+ binding
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
1PZ7 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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