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| {{STRUCTURE_2iep| PDB=2iep | SCENE= }} | | {{STRUCTURE_2iep| PDB=2iep | SCENE= }} |
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| '''Crystal structure of immunoglobulin-like domains 1 and 2 of the receptor tyrosine kinase MuSK'''
| | ===Crystal structure of immunoglobulin-like domains 1 and 2 of the receptor tyrosine kinase MuSK=== |
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| ==Overview==
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| Muscle-specific kinase (MuSK) is a receptor tyrosine kinase expressed exclusively in skeletal muscle, where it is required for formation of the neuromuscular junction. MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. Here, we report the crystal structure of the agrin-responsive first and second immunoglobulin-like domains (Ig1 and Ig2) of the MuSK ectodomain at 2.2 A resolution. The structure reveals that MuSK Ig1 and Ig2 are Ig-like domains of the I-set subfamily, which are configured in a linear, semi-rigid arrangement. In addition to the canonical internal disulfide bridge, Ig1 contains a second, solvent-exposed disulfide bridge, which our biochemical data indicate is critical for proper folding of Ig1 and processing of MuSK. Two Ig1-2 molecules form a non-crystallographic dimer that is mediated by a unique hydrophobic patch on the surface of Ig1. Biochemical analyses of MuSK mutants introduced into MuSK(-/-) myotubes demonstrate that residues in this hydrophobic patch are critical for agrin-induced MuSK activation.
| | The line below this paragraph, {{ABSTRACT_PUBMED_17011580}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17011580 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_17011580}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Stiegler, A L.]] | | [[Category: Stiegler, A L.]] |
| [[Category: Beta-sandwich]] | | [[Category: Beta-sandwich]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 07:25:13 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 03:17:29 2008'' |
