4RP4

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

4RP4 の概要

• エントリーDOI: 10.2210/pdb4rp4/pdb
• 分子名称: Disks large 1 tumor suppressor protein, FORMIC ACID (3 entities in total)
• 機能のキーワード: nysgrc, structural genomics, psi-biology, new york structural genomics research consortium, scaffolding, antitumor protein
• 由来する生物種: Drosophila melanogaster (Fruit fly)
• 細胞内の位置: Cytoplasm : P31007
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 22910.27

構造登録者

Ghosh, A.,Almo, S.C.,New York Structural Genomics Research Consortium (NYSGRC) (登録日: 2014-10-29, 公開日: 2014-11-26, 最終更新日: 2023-09-20)

主引用文献

Ghosh, A.,Ramagopal, U.A.,Bonanno, J.B.,Brenowitz, M.,Almo, S.C.
Structures of the L27 Domain of Disc Large Homologue 1 Protein Illustrate a Self-Assembly Module.
Biochemistry, 57:1293-1305, 2018

PubMed Abstract: 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 β-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.

PubMed: 29261291
DOI: 10.1021/acs.biochem.7b01074

実験手法

X-RAY DIFFRACTION (1.42 Å)