Current Biology
DispatchSH3 Domains: Molecular ‘Velcro’1
Section snippets
Text
Many biological processes involve the formation of specific protein aggregates or complexes, a good example being the transduction of signals through the cytoplasm by receptors with tyrosine kinase activity. Receptor aggregation is initiated by ligands — usually hormones or growth factors — outside the cell; inside the cell, phosphorylation-mediated protein association is crucial to the transmission of signals
Acknowledgements
We thank MRC, SERC, Wellcome and Zeneca for support and the Ludwig Institute in London for valuable collaborations.
C.J. Morton and I.D. Campbell, Oxford Centre for Molecular Sciences and Department of Biochemistry, South Parks Road, Oxford OX1 3QY, UK.
References (18)
- et al.
SH2 and SH3 domains
Curr Biol
(1993) - et al.
The crystal structure of human Csk SH3: structural diversity near the RT-Src and n-Src loop
FEBS Lett
(1994) - et al.
Solution structure of the SH3 domain of phospholipase C-γ
Cell
(1993) - et al.
Solution structure and ligand-binding site of the SH3 domain of the p85α subunit of phosphatidylinositol 3-kinase
Cell
(1993) - et al.
The GTPase dynamin binds to and is activated by a subset of SH3 domains
Cell
(1993) - et al.
Structural basis for the binding of proline-rich peptides to SH3 domains
Cell
(1994) - et al.
Crystal structure of a Src-homology 3 (SH3) domain
Nature
(1992) - et al.
Solution structure of the SH3 domain of Src and identification of its ligand binding site
Science
(1992)
Cited by (77)
Evolutionary Modeling of Protein Families by Chromosomal Translocation Events
2021, New Horizons in EvolutionThe Small β-Barrel Domain: A Survey-Based Structural Analysis
2019, StructureCitation Excerpt :Also, many SBB domains are fused or embedded within larger proteins. As two examples, note that (1) many kinases contain an SH3 domain (Morton and Campbell, 1994), and other proteins involved in signal-recognition contain SH3-like Tudor and Chromo domains (Blus et al., 2011), while (2) the RNA-binding ribosomal protein L2 consists of two fused SBB domains, with the N-terminal region adopting an OB fold and the C-terminal half being an SH3-like barrel (Diedrich et al., 2000). Once the whole is divided, the parts need names.
SH3 dependent cell death signaling of the avian chB6 alloantigen
2017, Cellular ImmunologyCitation Excerpt :This cytoplasmic domain is notably rich in proline residues [23] and acidic residues but has no tyrosine residues. SH3 binding sites are known to mediate wide variety of signals which includes different growth signals and are also known to be involved in apoptosis [33–36]. There are interesting parallels between chB6 and CD2.
A large scale huntingtin protein interaction network implicates RHO GTPase signaling pathways in huntington disease
2014, Journal of Biological ChemistryCitation Excerpt :The SH2 domain is mainly found in adaptor proteins and recognizes tyrosine-phosphorylated sites involved in intracellular signaling cascades (60). SH3 domains are also present in adaptor proteins that link partners with their respective PRRs (61). Like the WW domain, SH3 has been implicated in HD pathogenesis through its interaction with the PRR of HTT.
SPTBN1 Mediates the Cytoplasmic Constraint of PTTG1, Impairing Its Oncogenic Activity in Human Seminoma
2023, International Journal of Molecular Sciences
C.J. Morton and I.D. Campbell, Oxford Centre for Molecular Sciences and Department of Biochemistry, South Parks Road, Oxford OX1 3QY, UK.