By Giovanni Cesareni (Editor), Mario Gimona (Editor), Marius Sudol (Editor), Michael Yaffe (Editor)
Because the complete performance of any given protein can simply be understood when it comes to its interplay with different, usually regulatory proteins, this certain reference resource covers all correct protein domain names, together with SH2, SH3, PDZ, WW, PTB, EH, PH and PX. Its user-oriented idea combines huge assurance with effortless retrieval of crucial info, and contains a distinctive part on Web-based instruments and databases overlaying protein modules and sensible peptide motifs.Essential for the examine of protein-protein interactions in vivo or in silico, and a prerequisite for winning useful proteomics stories.
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Additional resources for Modular Protein Domains
Science 1991, 252, 668–674. , Assembly of cell regulatory systems through protein interaction domains. Science 2003, 300, 445–452. Tong, A. , A combined experimental and computational strategy to define protein interaction networks for peptide recognition modules. Science 2002, 295, 321–324. , Modular peptide recognition domains in eukaryotic signaling. Annu. Rev. Biophys. Biomol. Struct. 1997, 26, 259–288. Bradshaw, J. , Molecular recognition by SH2 domains. Adv. Protein Chem. 2002, 61, 161–210.
To explore the biological effects of this specificity switch, we made use of the fact that inactivation of the Grb2 gene in Caenorhabditis elegans (called sem-5) results in multiple defects, including abnormal development of the vulva, which can be rescued by reexpression of wild-type Grb2. We replaced the SH2 domain of Grb2 with that from Src and found that the chimeric Src-Grb2 adaptor, in which the Src SH2 domain is flanked by the Grb2 SH3 domains, was inefficient in rescuing the defect caused by loss of the endogenous gene.
In this example, an SH2-mediated interaction is designed to be weak, so that it can be readily reversed. Similarly, although specificity in protein–protein interactions is biologically important, there is often significant flexibility in the binding of interaction domains to their targets. A given SH2 domain may interact physiologically with phosphorylated sites on multiple different proteins, which may allow for cell-specific functions or the formation of more complex signaling networks within a single cell .