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4rp4

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Revision as of 05:08, 25 August 2022

Crystal Structure of the L27 domain of Discs Large 1 (target ID NYSGRC-010766) from Drosophila melanogaster (space group P212121)

Structural highlights

4rp4 is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.^[1] ^[2] ^[3]

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^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Bilder D, Li M, Perrimon N. Cooperative regulation of cell polarity and growth by Drosophila tumor suppressors. Science. 2000 Jul 7;289(5476):113-6. PMID:10884224
↑ Mendoza C, Olguin P, Lafferte G, Thomas U, Ebitsch S, Gundelfinger ED, Kukuljan M, Sierralta J. Novel isoforms of Dlg are fundamental for neuronal development in Drosophila. J Neurosci. 2003 Mar 15;23(6):2093-101. PMID:12657668
↑ Woods DF, Bryant PJ. The discs-large tumor suppressor gene of Drosophila encodes a guanylate kinase homolog localized at septate junctions. Cell. 1991 Aug 9;66(3):451-64. PMID:1651169
↑ Ghosh A, Ramagopal UA, Bonanno JB, Brenowitz M, Almo SC. Structures of the L27 Domain of Disc Large Homologue 1 Protein Illustrate a Self-Assembly Module. Biochemistry. 2018 Feb 27;57(8):1293-1305. doi: 10.1021/acs.biochem.7b01074. Epub, 2018 Feb 7. PMID:29261291 doi:http://dx.doi.org/10.1021/acs.biochem.7b01074

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4rp4"

@@ Line 1: / Line 1: @@
 ==Crystal Structure of the L27 domain of Discs Large 1 (target ID NYSGRC-010766) from Drosophila melanogaster (space group P212121)==
-<StructureSection load='4rp4' size='340' side='right' caption='[[4rp4]], [[Resolution|resolution]] 1.42&Aring;' scene=''>
+<StructureSection load='4rp4' size='340' side='right'caption='[[4rp4]], [[Resolution|resolution]] 1.42&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4rp4]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RP4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RP4 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4rp4]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RP4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RP4 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CG1725, Discs Large 1 Isoform B, dlg1, l(1)dlg1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</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=4rp4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rp4 OCA], [https://pdbe.org/4rp4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rp4 RCSB], [https://www.ebi.ac.uk/pdbsum/4rp4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rp4 ProSAT]</span></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=4rp4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rp4 OCA], [http://pdbe.org/4rp4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4rp4 RCSB], [http://www.ebi.ac.uk/pdbsum/4rp4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4rp4 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://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>
+[[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 ==
@@ Line 23: / Line 22: @@
 __TOC__
 </StructureSection>
-[[Category: Drome]]
+[[Category: Large Structures]]
 [[Category: Almo, S C]]
 [[Category: Ghosh, A]]

4rp4

From Proteopedia

Revision as of 05:08, 25 August 2022

Crystal Structure of the L27 domain of Discs Large 1 (target ID NYSGRC-010766) from Drosophila melanogaster (space group P212121)

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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