Kinetic Study of Human Full-Length Wild-Type JAK2 and V617F Mutant Proteins

D. Erdmann, B. Allard, J. Bohn, A. Pover, A. Floersheimer, Patrizia Fontana, M. Gerspacher, J. Hau, F. Hofmann, T. Radimerski, Roman Wille, C. Zimmermann, P. Chène
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引用次数: 8

Abstract

The Janus kinase 2 (JAK2) is a drug target in particular because a missense mutation in this gene (V617F) has been identified in various human diseases. We report here the first kinetic study of the human full-length wild type and V617F JAK2 proteins and of their isolated kinase domain. The kinetic parameters of both full-length proteins are similar revealing that the mutation does not affect JAK2 catalytic activity suggesting that it has a more complex role in the regu- lation of JAK2 activity. Our study also shows that the domains located outside the kinase domain have little influence on JAK2 catalytical activity.
人JAK2和V617F全长野生型突变蛋白的动力学研究
Janus激酶2 (JAK2)是一个特别的药物靶点,因为该基因(V617F)的错义突变已在各种人类疾病中被发现。我们在这里报道了人类全长野生型和V617F JAK2蛋白及其分离的激酶结构域的首次动力学研究。两种全长蛋白的动力学参数相似,表明突变不影响JAK2的催化活性,这表明它在JAK2活性的调节中具有更复杂的作用。我们的研究还表明,位于激酶结构域外的结构域对JAK2的催化活性影响不大。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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