1eg4

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[[Image:1eg4.jpg|left|200px]]
 
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==STRUCTURE OF A DYSTROPHIN WW DOMAIN FRAGMENT IN COMPLEX WITH A BETA-DYSTROGLYCAN PEPTIDE==
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The line below this paragraph, containing "STRUCTURE_1eg4", creates the "Structure Box" on the page.
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<StructureSection load='1eg4' size='340' side='right'caption='[[1eg4]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1eg4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EG4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EG4 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1eg4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eg4 OCA], [https://pdbe.org/1eg4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eg4 RCSB], [https://www.ebi.ac.uk/pdbsum/1eg4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eg4 ProSAT]</span></td></tr>
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{{STRUCTURE_1eg4| PDB=1eg4 | SCENE= }}
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/DAG1_HUMAN DAG1_HUMAN] Defects in DAG1 are the cause of muscular dystrophy-dystroglycanopathy limb-girdle type C7 (MDDGC7) [MIM:[https://omim.org/entry/613818 613818]. An autosomal recessive muscular dystrophy showing onset in early childhood, and associated with mental retardation without structural brain anomalies. Note=MDDGC7 is caused by DAG1 mutations that interfere with normal post-translational processing, resulting in defective DAG1 glycosylation and impaired interactions with extracellular-matrix components. Other muscular dystrophy-dystroglycanopathies are caused by defects in enzymes involved in protein O-glycosylation.<ref>PMID:21388311</ref>
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== Function ==
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[https://www.uniprot.org/uniprot/DAG1_HUMAN DAG1_HUMAN] The dystroglycan complex is involved in a number of processes including laminin and basement membrane assembly, sarcolemmal stability, cell survival, peripheral nerve myelination, nodal structure, cell migration, and epithelial polarization.<ref>PMID:9851927</ref> <ref>PMID:11724572</ref> <ref>PMID:16254364</ref> <ref>PMID:17360738</ref> Alpha-dystroglycan is an extracellular peripheral glycoprotein that acts as a receptor for both extracellular matrix proteins containing laminin-G domains, and for certain adenoviruses. Receptor for laminin-2 (LAMA2) and agrin in peripheral nerve Schwann cells. Also acts as a receptor for M.leprae in peripheral nerve Schwann cells but only in the presence of the G-domain of LAMA2, and for lymphocytic choriomeningitis virus, Old World Lassa fever virus, and clade C New World arenaviruses.<ref>PMID:9851927</ref> <ref>PMID:11724572</ref> <ref>PMID:16254364</ref> <ref>PMID:17360738</ref> Beta-dystroglycan is a transmembrane protein that plays important roles in connecting the extracellular matrix to the cytoskeleton. Acts as a cell adhesion receptor in both muscle and non-muscle tissues. Receptor for both DMD and UTRN and, through these interactions, scaffolds axin to the cytoskeleton. Also functions in cell adhesion-mediated signaling and implicated in cell polarity.<ref>PMID:9851927</ref> <ref>PMID:11724572</ref> <ref>PMID:16254364</ref> <ref>PMID:17360738</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/eg/1eg4_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1eg4 ConSurf].
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<div style="clear:both"></div>
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'''STRUCTURE OF A DYSTROPHIN WW DOMAIN FRAGMENT IN COMPLEX WITH A BETA-DYSTROGLYCAN PEPTIDE'''
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==See Also==
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*[[Dystrophin|Dystrophin]]
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== References ==
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==Overview==
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<references/>
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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.
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__TOC__
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</StructureSection>
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==About this Structure==
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1EG4 is a [[Protein complex]] structure of sequences 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=1EG4 OCA].
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==Reference==
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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]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Eck, M J.]]
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[[Category: Eck MJ]]
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[[Category: Huang, X.]]
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[[Category: Huang X]]
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[[Category: Joachimiak, A.]]
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[[Category: Joachimiak A]]
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[[Category: Poy, F.]]
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[[Category: Poy F]]
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[[Category: Sudol, M.]]
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[[Category: Sudol M]]
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[[Category: Zhang, R.]]
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[[Category: Zhang R]]
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[[Category: Ef-hand like domain]]
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[[Category: Ww domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:03:36 2008''
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Current revision

STRUCTURE OF A DYSTROPHIN WW DOMAIN FRAGMENT IN COMPLEX WITH A BETA-DYSTROGLYCAN PEPTIDE

PDB ID 1eg4

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