View source for 4rp5


==Crystal Structure of the L27 domain of Discs Large 1 (target ID NYSGRC-010766) from Drosophila melanogaster (space group P21)==
<StructureSection load='4rp5' size='340' side='right'caption='[[4rp5]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4rp5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RP5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RP5 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.65&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4rp5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rp5 OCA], [https://pdbe.org/4rp5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rp5 RCSB], [https://www.ebi.ac.uk/pdbsum/4rp5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rp5 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/DLG1_DROME DLG1_DROME] During embryonic development, some isoforms are essential for proper neuronal differentiation and organization. Required for cell polarity; maintenance of apicobasal polarity. Plays a critical role at septate junctions in cellular growth control during larval development. The presence of a guanylate kinase domain suggests involvement in cellular adhesion as well as signal transduction to control cellular proliferation.<ref>PMID:10884224</ref> <ref>PMID:12657668</ref> <ref>PMID:1651169</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Disc large 1 (Dlg1) proteins, members of the MAGUK protein family, are linked to cell polarity via their participation in multiprotein assemblies. At their N-termini, Dlg1 proteins contain a L27 domain. Typically, the L27 domains participate in the formation of obligate hetero-oligomers with the L27 domains from their cognate partners. Among the MAGUKs, Dlg1 proteins exist as homo-oligomers, and the oligomerization is solely dependent on the L27 domain. Here we provide biochemical and structural evidence of homodimerization via the L27 domain of Dlg1 from Drosophila melanogaster. The structure reveals that the core of the dimer is formed by a distinctive six-helix assembly, involving all three conserved helices from each subunit (monomer). The homodimer interface is extended by the C-terminal tail of the L27 domain of Dlg1, which forms a two-stranded antiparallel beta-sheet. The structure reconciles and provides a structural context for a large body of available mutational data. From our analyses, we conclude that the observed L27 homodimerization is most likely a feature unique to the Dlg1 orthologs within the MAGUK family.

Structures of the L27 Domain of Disc Large Homologue 1 Protein Illustrate a Self-Assembly Module.,Ghosh A, Ramagopal UA, Bonanno JB, Brenowitz M, Almo SC Biochemistry. 2018 Feb 27;57(8):1293-1305. doi: 10.1021/acs.biochem.7b01074. Epub, 2018 Feb 7. PMID:29261291<ref>PMID:29261291</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 4rp5" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Drosophila melanogaster]]
[[Category: Large Structures]]
[[Category: Almo SC]]
[[Category: Ghosh A]]