1q56

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(New page: 200px<br /><applet load="1q56" size="450" color="white" frame="true" align="right" spinBox="true" caption="1q56" /> '''NMR structure of the B0 isoform of the agrin...)
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'''NMR structure of the B0 isoform of the agrin G3 domain in its Ca2+ bound state'''<br />
'''NMR structure of the B0 isoform of the agrin G3 domain in its Ca2+ bound state'''<br />
==Overview==
==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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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==
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1Q56 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Q56 OCA].
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1Q56 is a [http://en.wikipedia.org/wiki/Single_protein 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==
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[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Alexandrescu, A.T.]]
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[[Category: Alexandrescu, A T.]]
[[Category: Frank, S.]]
[[Category: Frank, S.]]
[[Category: Jenny, M.]]
[[Category: Jenny, M.]]
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[[Category: Kammerer, R.A.]]
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[[Category: Kammerer, R A.]]
[[Category: Landwehr, R.]]
[[Category: Landwehr, R.]]
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[[Category: Maciejewski, M.W.]]
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[[Category: Maciejewski, M W.]]
[[Category: Rathgeb-Szabo, K.]]
[[Category: Rathgeb-Szabo, K.]]
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[[Category: Ruegg, M.A.]]
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[[Category: Ruegg, M A.]]
[[Category: Schulthess, T.]]
[[Category: Schulthess, T.]]
[[Category: Stetefeld, J.]]
[[Category: Stetefeld, J.]]
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[[Category: nmj synapse]]
[[Category: nmj synapse]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:23:30 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:35:57 2008''

Revision as of 12:36, 21 February 2008

Image:1q56.jpg

1q56

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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

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