Pin1 变异体的活性和亲和力。
Activity and Affinity of Pin1 Variants.
机构信息
Department of Biochemistry and Molecular Genetics, University of Colorado Anschutz Medical Campus, 12801 East 17th Avenue, Aurora, CO 80045, USA.
Faculty of Pharmacy, Mansoura University, Mansoura 35516, Egypt.
出版信息
Molecules. 2019 Dec 20;25(1):36. doi: 10.3390/molecules25010036.
Pin1 is a peptidyl-prolyl isomerase responsible for isomerizing phosphorylated S/T-P motifs. Pin1 has two domains that each have a distinct ligand binding site, but only its PPIase domain has catalytic activity. Vast evidence supports interdomain allostery of Pin1, with binding of a ligand to its regulatory WW domain impacting activity in the PPIase domain. Many diverse studies have made mutations in Pin1 in order to elucidate interactions that are responsible for ligand binding, isomerase activity, and interdomain allostery. Here, we summarize these mutations and their impact on Pin1's structure and function.
Pin1 是一种肽基脯氨酰顺反异构酶，负责异构磷酸化的 S/T-P 基序。Pin1 有两个结构域，每个结构域都有一个独特的配体结合位点，但只有其 PPIase 结构域具有催化活性。大量证据支持 Pin1 的结构域间变构，配体与其调节性 WW 结构域的结合会影响 PPIase 结构域的活性。许多不同的研究已经对 Pin1 进行了突变，以阐明负责配体结合、异构酶活性和结构域间变构的相互作用。在这里，我们总结了这些突变及其对 Pin1 结构和功能的影响。
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