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
{"title":"Kinetic Study of Human Full-Length Wild-Type JAK2 and V617F Mutant Proteins","authors":"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","doi":"10.2174/1874940200801010080","DOIUrl":null,"url":null,"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.","PeriodicalId":89033,"journal":{"name":"The open enzyme inhibition journal","volume":"1 1","pages":"80-84"},"PeriodicalIF":0.0000,"publicationDate":"2009-01-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"8","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"The open enzyme inhibition journal","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.2174/1874940200801010080","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
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.