Abstract：
The Proviral Integration of Molony murine leukemia virus (PIM)-1 protein contributes to the solid cancers and hematologic malignancies, cell growth, proliferation, differentiation, migration, and other life activities. Many studies have related these functions to its molecular structure, subcellular localization and expression level. However, recognition of specific active sites and their effects on the activity of this constitutively active kinase is still a challenge. Based on the close relationship between its molecular structure and functional activity, this review covers the specific residues involved in the binding of ATP and different substrates in its catalytic domain. This review then elaborates on the relevant changes in protein conformation and cell functions after PIM-1 binds to different substrates. Therefore, this intensive study can improve the understanding of PIM-1-regulated signaling pathways by facilitating the discovery of its potential phosphorylation substrates.
摘要：
Molony鼠白血病病毒（PIM）-1蛋白的前病毒整合有助于实体癌和血液系统恶性肿瘤，细胞生长,扩散,分化,迁移,和其他生命活动。许多研究已经将这些功能与其分子结构联系起来,亚细胞定位和表达水平。然而,识别特定的活性位点及其对这种组成型活性激酶活性的影响仍然是一个挑战。基于其分子结构与功能活性的密切关系,这篇综述涵盖了参与ATP与催化域中不同底物结合的特定残基。本文就PIM-1与不同底物结合后蛋白质构象和细胞功能的相关变化进行综述。因此,这项深入的研究可以通过促进发现PIM-1调节的信号通路潜在的磷酸化底物来提高对PIM-1调节的信号通路的理解.
