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1u2c

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==Crystal Structure of a-dystroglycan==
==Crystal Structure of a-dystroglycan==
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<StructureSection load='1u2c' size='340' side='right' caption='[[1u2c]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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<StructureSection load='1u2c' size='340' side='right'caption='[[1u2c]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1u2c]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U2C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1U2C FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1u2c]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U2C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1U2C FirstGlance]. <br>
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</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=1u2c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u2c OCA], [http://pdbe.org/1u2c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1u2c RCSB], [http://www.ebi.ac.uk/pdbsum/1u2c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1u2c ProSAT]</span></td></tr>
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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]] 2.3&#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=1u2c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u2c OCA], [https://pdbe.org/1u2c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1u2c RCSB], [https://www.ebi.ac.uk/pdbsum/1u2c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1u2c ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/DAG1_MOUSE DAG1_MOUSE]] The dystroglycan complex is involved in a number of processes including laminin and basement membrane assembly, sacrolemmal stability, cell survival, peripheral nerve myelination, nodal structure, cell migration, and epithelial polarization.<ref>PMID:9175728</ref> <ref>PMID:12843252</ref> <ref>PMID:12797959</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 receptor for lymphocytic choriomeningitis virus, Old World Lassa fever virus, and clade C New World arenaviruses.<ref>PMID:9175728</ref> <ref>PMID:12843252</ref> <ref>PMID:12797959</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 (By similarity).<ref>PMID:9175728</ref> <ref>PMID:12843252</ref> <ref>PMID:12797959</ref>
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[https://www.uniprot.org/uniprot/DAG1_MOUSE DAG1_MOUSE] The dystroglycan complex is involved in a number of processes including laminin and basement membrane assembly, sacrolemmal stability, cell survival, peripheral nerve myelination, nodal structure, cell migration, and epithelial polarization.<ref>PMID:9175728</ref> <ref>PMID:12843252</ref> <ref>PMID:12797959</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 receptor for lymphocytic choriomeningitis virus, Old World Lassa fever virus, and clade C New World arenaviruses.<ref>PMID:9175728</ref> <ref>PMID:12843252</ref> <ref>PMID:12797959</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 (By similarity).<ref>PMID:9175728</ref> <ref>PMID:12843252</ref> <ref>PMID:12797959</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=1u2c ConSurf].
</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=1u2c ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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Dystroglycan (DG) is a cell surface receptor consisting of two subunits: alpha-dystroglycan, extracellular and highly glycosylated, and beta-dystroglycan, spanning the cell membrane. It is a pivotal member of the dystrophin-glycoprotein complex and is involved in a wide variety of important cellular processes such as the stabilization of the muscle fiber sarcolemma or the clustering of acetylcholine receptors. We report the 2.3-A resolution crystal structure of the murine skeletal muscle N-terminal alpha-DG region, which confirms the presence of two autonomous domains; the first finally identified as an Ig-like and the second resembling ribosomal RNA-binding proteins. Solid-phase laminin binding assays show the occurrence of protein-protein type of interactions involving the Ig-like domain of alpha-DG.
 
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The structure of the N-terminal region of murine skeletal muscle alpha-dystroglycan discloses a modular architecture.,Bozic D, Sciandra F, Lamba D, Brancaccio A J Biol Chem. 2004 Oct 22;279(43):44812-6. Epub 2004 Aug 23. PMID:15326183<ref>PMID:15326183</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 1u2c" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Lk3 transgenic mice]]
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[[Category: Large Structures]]
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[[Category: Bozic, D]]
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[[Category: Mus musculus]]
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[[Category: Brancaccio, A]]
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[[Category: Bozic D]]
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[[Category: Lamba, D]]
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[[Category: Brancaccio A]]
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[[Category: Sciandra, F]]
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[[Category: Lamba D]]
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[[Category: Ig-like domain]]
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[[Category: Sciandra F]]
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[[Category: Protein binding]]
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[[Category: S6 like fold]]
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Current revision

Crystal Structure of a-dystroglycan

PDB ID 1u2c

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