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Recombinant thrombin receptor and related pharmaceuticals
Recombinant thrombin receptor and related pharmaceuticals

... far, Whether proteolytic cleavage by thrombin is involved in ...
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Src protein–tyrosine kinase structure and regulation

... surface of the SH2 domain and point toward basic residues on the surface. The Src SH2 domain, however, can bind to a variety of sequences that do not conform to this optimal sequence, and other parts of proteins beyond the vicinity of the phosphotyrosine contribute to binding affinity. The human Src g ...
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Catalytic triad



A catalytic triad refers to the three amino acid residues that function together at the centre of the active site of some hydrolase and transferase enzymes (e.g. proteases, amidases, esterases, acylases, lipases and β-lactamases). An Acid-Base-Nucleophile triad is a common motif for generating a nucleophilic residue for covalent catalysis. The residues form a charge-relay network to polarise and activate the nucleophile, which attacks the substrate, forming a covalent intermediate which is then hydrolysed to regenerate free enzyme. The nucleophile is most commonly a serine or cysteine amino acid, but occasionally threonine. Because enzymes fold into complex three-dimensional structures, the residues of a catalytic triad can be far from each other along the amino-acid sequence (primary structure), however, they are brought close together in the final fold.As well as divergent evolution of function (and even the triad's nucleophile), catalytic triads show some of the best examples of convergent evolution. Chemical constraints on catalysis have led to the same catalytic solution independently evolving in at least 23 separate superfamilies. Their mechanism of action is consequently one of the best studied in biochemistry.
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