1pz8: Difference between revisions
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|PDB= 1pz8 |SIZE=350|CAPTION= <scene name='initialview01'>1pz8</scene>, resolution 2.35Å | |PDB= 1pz8 |SIZE=350|CAPTION= <scene name='initialview01'>1pz8</scene>, resolution 2.35Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= AGRN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9031 Gallus gallus]) | |GENE= AGRN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9031 Gallus gallus]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1pz7|1PZ7]], [[1q56|1Q56]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1pz8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pz8 OCA], [http://www.ebi.ac.uk/pdbsum/1pz8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1pz8 RCSB]</span> | |||
}} | }} | ||
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[[Category: Schulthess, T.]] | [[Category: Schulthess, T.]] | ||
[[Category: Stetefeld, J.]] | [[Category: Stetefeld, J.]] | ||
[[Category: agrin]] | [[Category: agrin]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:06:41 2008'' | ||
Revision as of 23:06, 30 March 2008
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| , resolution 2.35Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | AGRN (Gallus gallus) | ||||||
| Related: | 1PZ7, 1Q56
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Modulation of agrin function by alternative splicing and Ca2+ binding
OverviewOverview
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 StructureAbout this Structure
1PZ8 is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.
ReferenceReference
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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