1pz7
From Proteopedia
(New page: 200px<br /><applet load="1pz7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pz7, resolution 1.421Å" /> '''Modulation of agrin...) |
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| - | [[Image:1pz7.jpg|left|200px]]<br /><applet load="1pz7" size=" | + | [[Image:1pz7.jpg|left|200px]]<br /><applet load="1pz7" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1pz7, resolution 1.421Å" /> | caption="1pz7, resolution 1.421Å" /> | ||
'''Modulation of agrin function by alternative splicing and Ca2+ binding'''<br /> | '''Modulation of agrin function by alternative splicing and Ca2+ binding'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The aggregation of acetylcholine receptors on postsynaptic membranes is a | + | 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== | ==About this Structure== | ||
| - | 1PZ7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1PZ7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PZ7 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Gallus gallus]] | [[Category: Gallus gallus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Alexandrescu, A | + | [[Category: Alexandrescu, A T.]] |
[[Category: Frank, S.]] | [[Category: Frank, S.]] | ||
[[Category: Jenny, M.]] | [[Category: Jenny, M.]] | ||
| - | [[Category: Kammerer, R | + | [[Category: Kammerer, R A.]] |
[[Category: Landwehr, R.]] | [[Category: Landwehr, R.]] | ||
| - | [[Category: Maciejewski, M | + | [[Category: Maciejewski, M W.]] |
[[Category: Rathgeb-Szabo, K.]] | [[Category: Rathgeb-Szabo, K.]] | ||
| - | [[Category: Ruegg, M | + | [[Category: Ruegg, M A.]] |
[[Category: Schulthess, T.]] | [[Category: Schulthess, T.]] | ||
[[Category: Stetefeld, J.]] | [[Category: Stetefeld, J.]] | ||
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[[Category: agrin]] | [[Category: agrin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:34:09 2008'' |
Revision as of 12:34, 21 February 2008
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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 with as ligand. 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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