GTP is an allosteric modulator of the interaction between the guanylate-binding protein 1 and the prosurvival kinase PIM1

被引：9
|
作者：
Persico, Marco [1 ]
Petrella, Lella [2 ]
Orteca, Nausicaa [1 ]
Di Dato, Antonio [1 ]
Mariani, Marisa [3 ]
Andreoli, Mirko [3 ]
De Donato, Marta [4 ]
Scambia, Giovanni [4 ]
Novellino, Ettore [1 ]
Ferlini, Cristiano [3 ]
Fattorusso, Caterina [1 ]
机构：
[1] Univ Naples Federico II, Dipartimento Farm, I-80131 Naples, Italy
[2] Jean Paul II Res Fdn, Mol Oncol Lab, I-86100 Campobasso, Italy
[3] Danbury Hosp Res Inst, Danbury, CT 06810 USA
[4] Univ Cattolica Sacro Cuore, Dept Obstet & Gynaecol, I-00168 Rome, Italy
来源：
EUROPEAN JOURNAL OF MEDICINAL CHEMISTRY | 2015年 / 91卷
关键词：
Human guanylate-binding protein 1; Paclitaxel resistance; GTPase activity; Protein conformational changes; Allosteric inhibition of protein protein interaction; NUCLEOTIDE-BINDING; HYDROLYSIS; MOLECULES; HGBP1; IDENTIFICATION; SIMULATIONS; EXPRESSION; RESISTANCE; INHIBITORS; MECHANISM;
D O I：
10.1016/j.ejmech.2014.07.093
中图分类号：
R914 [药物化学];
学科分类号：
100701 ;
摘要：
GBP1 and PIM1 are known to interact with a molar ratio 1:1. GBP1:PIM1 binding initiates a signaling pathway that induces resistance to common chemotherapeutics such as paclitaxel. Since GBP1 is a large GTPase which undergoes conformational changes in a nucleotide-dependent manner, we investigated the effect of GTP/GDP binding on GBP1:PIM1 interaction by using computational and biological studies. It resulted that only GTP decreases the formation of the GBP1:PIM1 complex through an allosteric mechanism, putting the bases for the identification of new compounds potentially able to revert resistance to paclitaxel. (C) 2014 Elsevier Masson SAS. All rights reserved.
引用
收藏
页码：132 / 144
页数：13
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