1eg3: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1eg3]] is a 1 chain structure with 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1EG3 FirstGlance]. <br> | <table><tr><td colspan='2'>[[1eg3]] is a 1 chain structure with 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1EG3 FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1eg4|1eg4]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1eg4|1eg4]]</td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1eg3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eg3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1eg3 RCSB], [http://www.ebi.ac.uk/pdbsum/1eg3 PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1eg3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eg3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1eg3 RCSB], [http://www.ebi.ac.uk/pdbsum/1eg3 PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Disease == | == Disease == | ||
[[http://www.uniprot.org/uniprot/DMD_HUMAN DMD_HUMAN]] Defects in DMD are the cause of Duchenne muscular dystrophy (DMD) [MIM:[http://omim.org/entry/310200 310200]]. DMD is the most common form of muscular dystrophy; a sex-linked recessive disorder. It typically presents in boys aged 3 to 7 year as proximal muscle weakness causing waddling gait, toe-walking, lordosis, frequent falls, and difficulty in standing up and climbing up stairs. The pelvic girdle is affected first, then the shoulder girdle. Progression is steady and most patients are confined to a wheelchair by age of 10 or 12. Flexion contractures and scoliosis ultimately occur. About 50% of patients have a lower IQ than their genetic expectations would suggest. There is no treatment.<ref>PMID:8401582</ref> <ref>PMID:7981690</ref> <ref>PMID:8817332</ref> <ref>PMID:9851445</ref> Defects in DMD are the cause of Becker muscular dystrophy (BMD) [MIM:[http://omim.org/entry/300376 300376]]. BMD resembles DMD in hereditary and clinical features but is later in onset and more benign.<ref>PMID:10573008</ref> Defects in DMD are a cause of cardiomyopathy dilated X-linked type 3B (CMD3B) [MIM:[http://omim.org/entry/302045 302045]]; also known as X-linked dilated cardiomyopathy (XLCM). Dilated cardiomyopathy is a disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death.<ref>PMID:9170407</ref> <ref>PMID:12354438</ref> <ref>PMID:12359139</ref> | [[http://www.uniprot.org/uniprot/DMD_HUMAN DMD_HUMAN]] Defects in DMD are the cause of Duchenne muscular dystrophy (DMD) [MIM:[http://omim.org/entry/310200 310200]]. DMD is the most common form of muscular dystrophy; a sex-linked recessive disorder. It typically presents in boys aged 3 to 7 year as proximal muscle weakness causing waddling gait, toe-walking, lordosis, frequent falls, and difficulty in standing up and climbing up stairs. The pelvic girdle is affected first, then the shoulder girdle. Progression is steady and most patients are confined to a wheelchair by age of 10 or 12. Flexion contractures and scoliosis ultimately occur. About 50% of patients have a lower IQ than their genetic expectations would suggest. There is no treatment.<ref>PMID:8401582</ref> <ref>PMID:7981690</ref> <ref>PMID:8817332</ref> <ref>PMID:9851445</ref> Defects in DMD are the cause of Becker muscular dystrophy (BMD) [MIM:[http://omim.org/entry/300376 300376]]. BMD resembles DMD in hereditary and clinical features but is later in onset and more benign.<ref>PMID:10573008</ref> Defects in DMD are a cause of cardiomyopathy dilated X-linked type 3B (CMD3B) [MIM:[http://omim.org/entry/302045 302045]]; also known as X-linked dilated cardiomyopathy (XLCM). Dilated cardiomyopathy is a disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death.<ref>PMID:9170407</ref> <ref>PMID:12354438</ref> <ref>PMID:12359139</ref> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Eck, M J | [[Category: Eck, M J]] | ||
[[Category: Huang, X | [[Category: Huang, X]] | ||
[[Category: Joachimiak, A | [[Category: Joachimiak, A]] | ||
[[Category: Poy, F | [[Category: Poy, F]] | ||
[[Category: Sudol, M | [[Category: Sudol, M]] | ||
[[Category: Zhang, R | [[Category: Zhang, R]] | ||
[[Category: Ef-hand like domain]] | [[Category: Ef-hand like domain]] | ||
[[Category: Structural protein]] | [[Category: Structural protein]] | ||
[[Category: Ww domain]] | [[Category: Ww domain]] | ||
Revision as of 21:23, 22 December 2014
STRUCTURE OF A DYSTROPHIN WW DOMAIN FRAGMENT IN COMPLEX WITH A BETA-DYSTROGLYCAN PEPTIDESTRUCTURE OF A DYSTROPHIN WW DOMAIN FRAGMENT IN COMPLEX WITH A BETA-DYSTROGLYCAN PEPTIDE
Structural highlights
Disease[DMD_HUMAN] Defects in DMD are the cause of Duchenne muscular dystrophy (DMD) [MIM:310200]. DMD is the most common form of muscular dystrophy; a sex-linked recessive disorder. It typically presents in boys aged 3 to 7 year as proximal muscle weakness causing waddling gait, toe-walking, lordosis, frequent falls, and difficulty in standing up and climbing up stairs. The pelvic girdle is affected first, then the shoulder girdle. Progression is steady and most patients are confined to a wheelchair by age of 10 or 12. Flexion contractures and scoliosis ultimately occur. About 50% of patients have a lower IQ than their genetic expectations would suggest. There is no treatment.[1] [2] [3] [4] Defects in DMD are the cause of Becker muscular dystrophy (BMD) [MIM:300376]. BMD resembles DMD in hereditary and clinical features but is later in onset and more benign.[5] Defects in DMD are a cause of cardiomyopathy dilated X-linked type 3B (CMD3B) [MIM:302045]; also known as X-linked dilated cardiomyopathy (XLCM). Dilated cardiomyopathy is a disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death.[6] [7] [8] Function[DMD_HUMAN] Anchors the extracellular matrix to the cytoskeleton via F-actin. Ligand for dystroglycan. Component of the dystrophin-associated glycoprotein complex which accumulates at the neuromuscular junction (NMJ) and at a variety of synapses in the peripheral and central nervous systems and has a structural function in stabilizing the sarcolemma. Also implicated in signaling events and synaptic transmission.[9] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedDystrophin 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. 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[10] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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