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[[Image:1u2c.jpg|left|200px]]


{{Structure
==Crystal Structure of a-dystroglycan==
|PDB= 1u2c |SIZE=350|CAPTION= <scene name='initialview01'>1u2c</scene>, resolution 2.30&Aring;
<StructureSection load='1u2c' size='340' side='right'caption='[[1u2c]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND=  
<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>
|ACTIVITY=  
</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>
|GENE=  
<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>
|DOMAIN=
</table>
|RELATEDENTRY=
== Function ==
|RESOURCES=<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://www.ebi.ac.uk/pdbsum/1u2c PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1u2c RCSB]</span>
[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 ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/u2/1u2c_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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>


'''Crystal Structure of a-dystroglycan'''
==See Also==
 
*[[Dystroglycan|Dystroglycan]]
 
== References ==
==Overview==
<references/>
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.
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Large Structures]]
1U2C is a [[Single protein]] structure of sequence from [http://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].
 
==Reference==
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:[http://www.ncbi.nlm.nih.gov/pubmed/15326183 15326183]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Bozic D]]
[[Category: Bozic, D.]]
[[Category: Brancaccio A]]
[[Category: Brancaccio, A.]]
[[Category: Lamba D]]
[[Category: Lamba, D.]]
[[Category: Sciandra F]]
[[Category: Sciandra, F.]]
[[Category: ig-like domain]]
[[Category: s6 like fold]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:04:25 2008''

Latest revision as of 08:46, 1 May 2024

Crystal Structure of a-dystroglycan

1u2c, resolution 2.30Å

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