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parvulin 的 42kDa 结构分析

Structural Analysis of the 42 kDa Parvulin of .

机构信息

University Duisburg-Essen, Research Group Structural and Medicinal Biochemistry, Centre for Medical Biotechnology (ZMB), University of Duisburg-Essen, 45117 Essen, Germany.

Protein Crystallography, Faculty of Biology and Biotechnology, Ruhr University Bochum, 44801 Bochum, Germany.

出版信息

Biomolecules. 2019 Mar 7;9(3):93. doi: 10.3390/biom9030093.

Abstract

is a unicellular eukaryotic parasite, which causes the African sleeping sickness in humans. The recently discovered trypanosomal protein Parvulin 42 (Par42) plays a key role in parasite cell proliferation. Homologues of this two-domain protein are exclusively found in protozoa species. Par42 exhibits an N-terminal forkhead associated (FHA)-domain and a peptidyl-prolyl--isomerase (PPIase) domain, both connected by a linker. Using NMR and X-ray analysis as well as activity assays, we report on the structures of the single domains of Par42, discuss their intra-molecular interplay, and give some initial hints as to potential cellular functions of the protein.

摘要

是一种单细胞真核寄生虫,会导致人类患上非洲昏睡病。最近发现的锥虫蛋白 Parvulin 42(Par42)在寄生虫细胞增殖中起着关键作用。这种具有两个结构域的蛋白的同源物仅存在于原生动物物种中。Par42 表现出一个 N 端与叉头相关(FHA)结构域和一个肽基脯氨酰--异构酶(PPIase)结构域,两者通过一个接头连接。我们使用 NMR 和 X 射线分析以及活性测定报告了 Par42 的单个结构域的结构,讨论了它们的分子内相互作用,并初步提示了该蛋白的潜在细胞功能。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c61b/6468809/84099ef8a9bf/biomolecules-09-00093-g001.jpg

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