1eg4

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{{Seed}}
 
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[[Image:1eg4.png|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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== 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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</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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__TOC__
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(as it appears on PubMed at http://www.pubmed.gov), where 10932245 is the PubMed ID number.
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</StructureSection>
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{{ABSTRACT_PUBMED_10932245}}
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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 Tue Jul 1 00:38:44 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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