1pz7

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{{STRUCTURE_1pz7| PDB=1pz7 | SCENE= }}
{{STRUCTURE_1pz7| PDB=1pz7 | SCENE= }}
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'''Modulation of agrin function by alternative splicing and Ca2+ binding'''
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===Modulation of agrin function by alternative splicing and Ca2+ binding===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_15016366}}
==About this Structure==
==About this Structure==
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[[Category: Stetefeld, J.]]
[[Category: Stetefeld, J.]]
[[Category: Agrin]]
[[Category: Agrin]]
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Revision as of 18:14, 28 July 2008

Image:1pz7.png

Template:STRUCTURE 1pz7

Modulation of agrin function by alternative splicing and Ca2+ binding

Template:ABSTRACT PUBMED 15016366

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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