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Crystal structure of human dipeptidyl peptidase IV/CD26 in complex with a substrate analog

机译:人二肽基肽酶IV / CD26与底物类似物的晶体结构

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Dipeptidyl peptidase IV (DPP-IV/CD26) is a multifunctional type II transmembrane serine peptidase. This enzyme contributes to the regulation of various physiological processes, including blood sugar homeostasis, by cleaving peptide hormones, chemokines and neuropeptides. We have determined the 2.5 Angstrom structure of the extracellular region of DPP-IV in complex with the inhibitor valine-pyrrolidide. The catalytic site is located in a large cavity formed between the alpha/beta-hydrolase domain and an eight-bladed beta-propeller domain. Both domains participate in inhibitor binding. The structure indicates how substrate specificity is achieved and reveals a new and unexpected opening to the active site. [References: 35]
机译:二肽基肽酶IV(DPP-IV / CD26)是多功能的II型跨膜丝氨酸肽酶。该酶通过裂解肽激素,趋化因子和神经肽,有助于调节各种生理过程,包括血糖稳态。我们已经确定了与抑制剂缬氨酸-吡咯烷化物复合的DPP-IV胞外区的2.5埃结构。催化位点位于α/β-水解酶结构域和八叶β-螺旋桨结构域之间形成的大空腔中。两个结构域均参与抑制剂结合。该结构指示了如何实现底物特异性,并揭示了活性位点的新的和意外的开放。 [参考:35]

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