Solution structure of the SH3 domain of phospholipase C-gamma
Article Abstract:
The 2-dimensional 1H nuclear magnetic resonance analysis of the solution structure of the Src homology 3 (SH3) domain of human phospholipase C-gamma (PLC-gamma) is reported. SH3 domains are key components of intracellular signaling mechanisms, functioning as binding sites for cytoplasmic target proteins. The distinctive features of human PLC-gamma include its eight antiparallel beta strands consisting of two successive Greek-key motifs forming a barrel-like structure, and the aliphatic and aromatic residues forming a hydrophobic pocket on the surface of the molecule.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1993
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A lipid-anchored Grb2-binding protein that links FGF-receptor activation to the Ras/MAPK signaling pathway
Article Abstract:
The role of the Ras/mitogen-activated protein kinase (MAPK) signaling pathway and fibroblast growth factor (FGF) receptors in cell proliferation was analyzed by utilizing the FRS2 binding protein. The FRS2 protein was characterized as a tyrosine phosphorylated peptide that binds to Grb2/Sos in response to cellular signalling via FGF and neurotrophic growth factors. The membrane localization, tyrosine phosphorylation and MAPK activation of the novel protein was also initiated by myristylation in response to FGF stimulation.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1997
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Tertiary structure of destrin and structural similarity between two actin-regulating protein families
Article Abstract:
Tertiary structure studies of destrin, an isoprotein of cofilin, reveal similarity between folding in destrin and repeated segments in the gelsolin family. However, the amino acid sequences fail to show similarities. The dissimilarity in sequence in the actin-binding helix is responsible for the Ca(super 2+)-independent actin-binding of destrin. The possible mechanisms of nuclear translocation with actin and pH-dependent filament severing are discussed with respect to tertiary structure.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1996
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