Lohse D L, Denu J M, Dixon J E
Department of Biological Chemistry, University of Michigan Medical School, Ann Arbor 48109-0606, USA.
Structure. 1995 Oct 15;3(10):987-90. doi: 10.1016/s0969-2126(01)00234-9.
The crystal structures of serine/threonine phosphatases provide the basis for understanding their inhibition by physiologically relevant compounds such as microcystin, cyclosporin and FK506. The structures also highlight the importance of a common sequence motif found in a large family of metal-containing enzymes involved in phosphate ester hydrolysis.
丝氨酸/苏氨酸磷酸酶的晶体结构为理解其被诸如微囊藻毒素、环孢菌素和FK506等生理相关化合物抑制提供了基础。这些结构还突出了在参与磷酸酯水解的一大类含金属酶中发现的一个共同序列基序的重要性。