Department of Pharmacological Sciences, Stony Brook University, Stony Brook, NY 11794, U.S.A.
Biochem Soc Trans. 2023 Feb 27;51(1):373-385. doi: 10.1042/BST20220940.
The human genome encodes more than 500 different protein kinases: signaling enzymes with tightly regulated activity. Enzymatic activity within the conserved kinase domain is influenced by numerous regulatory inputs including the binding of regulatory domains, substrates, and the effect of post-translational modifications such as autophosphorylation. Integration of these diverse inputs occurs via allosteric sites that relate signals via networks of amino acid residues to the active site and ensures controlled phosphorylation of kinase substrates. Here, we review mechanisms of allosteric regulation of protein kinases and recent advances in the field.
人类基因组编码了超过 500 种不同的蛋白激酶：具有严格调控活性的信号酶。在保守的激酶结构域内，酶的活性受到许多调节输入的影响，包括调节结构域、底物的结合以及翻译后修饰（如自身磷酸化）的影响。这些不同的输入通过别构位点进行整合，通过氨基酸残基网络将信号传递到活性位点，并确保激酶底物的受控磷酸化。在这里，我们回顾了蛋白激酶别构调节的机制以及该领域的最新进展。
