BAIT

PLCB3

phospholipase C, beta 3 (phosphatidylinositol-specific)
GO Process (4)
GO Function (2)
GO Component (3)
Homo sapiens
PREY

GNAQ

1110005L02Rik, 6230401I02Rik, AA408290, AW060788, Dsk1, Dsk10, Galphaq, Gq, GqI
guanine nucleotide binding protein, alpha q polypeptide
GO Process (25)
GO Function (8)
GO Component (8)
Mus musculus

Co-crystal Structure

Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex.

Publication

Full-length Gα(q)-phospholipase C-β3 structure reveals interfaces of the C-terminal coiled-coil domain.

Lyon AM, Dutta S, Boguth CA, Skiniotis G, Tesmer JJ

Phospholipase C-β (PLCβ) is directly activated by Gαq, but the molecular basis for how its distal C-terminal domain (CTD) contributes to maximal activity is poorly understood. Herein we present both the crystal structure and cryo-EM three-dimensional reconstructions of human full-length PLCβ3 in complex with mouse Gαq. The distal CTD forms an extended monomeric helical bundle consisting of three antiparallel segments ... [more]

Nat. Struct. Mol. Biol. Mar. 01, 2013; 20(3);355-62 [Pubmed: 23377541]

Throughput

  • Low Throughput

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
PLCB3 GNAQ
Co-crystal Structure
Co-crystal Structure

Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex.

Low-BioGRID
908032

Curated By

  • BioGRID