1q56: Difference between revisions
New page: left|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... |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1q56.jpg|left|200px]]<br /><applet load="1q56" size=" | [[Image:1q56.jpg|left|200px]]<br /><applet load="1q56" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1q56" /> | caption="1q56" /> | ||
'''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== | ||
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== | ||
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:// | 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== | ||
| Line 13: | Line 13: | ||
[[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.]] | ||
| Line 31: | Line 31: | ||
[[Category: nmj synapse]] | [[Category: nmj synapse]] | ||
''Page seeded by [http:// | ''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
|
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
Page seeded by OCA on Thu Feb 21 14:35:57 2008
Proteopedia Page Contributors and Editors (what is this?)
- Pages with broken file links
- Gallus gallus
- Single protein
- Alexandrescu, A T.
- Frank, S.
- Jenny, M.
- Kammerer, R A.
- Landwehr, R.
- Maciejewski, M W.
- Rathgeb-Szabo, K.
- Ruegg, M A.
- Schulthess, T.
- Stetefeld, J.
- Achr aggregation
- Ca2+ regulation
- Conformational flexibility
- Laminin-g like domain
- Mrna splicing
- Musk activation
- Nmj synapse
