1eg3: Difference between revisions
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[[Image:1eg3.jpg|left|200px]] | [[Image:1eg3.jpg|left|200px]] | ||
'''STRUCTURE OF A DYSTROPHIN WW DOMAIN FRAGMENT IN COMPLEX WITH A BETA-DYSTROGLYCAN PEPTIDE''' | {{Structure | ||
|PDB= 1eg3 |SIZE=350|CAPTION= <scene name='initialview01'>1eg3</scene>, resolution 2.0Å | |||
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|LIGAND= | |||
|ACTIVITY= | |||
|GENE= | |||
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'''STRUCTURE OF A DYSTROPHIN WW DOMAIN FRAGMENT IN COMPLEX WITH A BETA-DYSTROGLYCAN PEPTIDE''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1EG3 is a [ | 1EG3 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EG3 OCA]. | ||
==Reference== | ==Reference== | ||
Structure of a WW domain containing fragment of dystrophin in complex with beta-dystroglycan., Huang X, Poy F, Zhang R, Joachimiak A, Sudol M, Eck MJ, Nat Struct Biol. 2000 Aug;7(8):634-8. PMID:[http:// | Structure of a WW domain containing fragment of dystrophin in complex with beta-dystroglycan., Huang X, Poy F, Zhang R, Joachimiak A, Sudol M, Eck MJ, Nat Struct Biol. 2000 Aug;7(8):634-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10932245 10932245] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: ww domain]] | [[Category: ww domain]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:55:09 2008'' | ||
Revision as of 11:55, 20 March 2008
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STRUCTURE OF A DYSTROPHIN WW DOMAIN FRAGMENT IN COMPLEX WITH A BETA-DYSTROGLYCAN PEPTIDE
OverviewOverview
Dystrophin and beta-dystroglycan are components of the dystrophin-glycoprotein complex (DGC), a multimolecular assembly that spans the cell membrane and links the actin cytoskeleton to the extracellular basal lamina. Defects in the dystrophin gene are the cause of Duchenne and Becker muscular dystrophies. The C-terminal region of dystrophin binds the cytoplasmic tail of beta-dystroglycan, in part through the interaction of its WW domain with a proline-rich motif in the tail of beta-dystroglycan. Here we report the crystal structure of this portion of dystrophin in complex with the proline-rich binding site in beta-dystroglycan. The structure shows that the dystrophin WW domain is embedded in an adjacent helical region that contains two EF-hand-like domains. The beta-dystroglycan peptide binds a composite surface formed by the WW domain and one of these EF-hands. Additionally, the structure reveals striking similarities in the mechanisms of proline recognition employed by WW domains and SH3 domains.
DiseaseDisease
Known diseases associated with this structure: Becker muscular dystrophy OMIM:[300377], Cardiomyopathy, dilated, 3B OMIM:[300377], Duchenne muscular dystrophy OMIM:[300377]
About this StructureAbout this Structure
1EG3 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Structure of a WW domain containing fragment of dystrophin in complex with beta-dystroglycan., Huang X, Poy F, Zhang R, Joachimiak A, Sudol M, Eck MJ, Nat Struct Biol. 2000 Aug;7(8):634-8. PMID:10932245
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