酪氨酸磷酸化在 PTP-PEST 中的作用

IF 2.9 2区化学 Q3 CHEMISTRY, PHYSICAL

The Journal of Physical Chemistry B Pub Date : 2024-10-31 Epub Date: 2024-10-18 DOI:10.1021/acs.jpcb.4c04047

Sreevidya Thirumalai Srinivasan, Amrutha Manikandan, Narayanan Manoj, Madhulika Dixit, Satyavani Vemparala

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引用次数: 0

摘要

我们研究了酪氨酸磷酸化对细胞膜蛋白酪氨酸磷酸酶 PTP-PEST 的影响。结合实验数据和计算建模，我们确定了可能发生磷酸化的特定酪氨酸位点，特别是 Y64 和 Y88。这些位点的磷酸化会影响催化位点附近的环路动力学，改变关键残基之间的相互作用，并改变结合袋的大小。这反过来又会影响底物的结合，如结合能的变化所示。我们的研究结果让我们深入了解了酪氨酸磷酸化对 PTP-PEST 的结构和功能影响，加深了我们对其对底物结合和催化构象影响的理解。

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Role of Tyrosine Phosphorylation in PTP-PEST.

We study the influence of tyrosine phosphorylation on PTP-PEST, a cytosolic protein tyrosine phosphatase. Utilizing a combination of experimental data and computational modeling, specific tyrosine sites, notably, Y64 and Y88, are identified for potential phosphorylation. Phosphorylation at these sites affects loop dynamics near the catalytic site, altering interactions among key residues and modifying the size of the binding pocket. This, in turn, impacts substrate binding, as indicated by changes in the binding energy. Our findings provide insights into the structural and functional consequences of tyrosine phosphorylation on PTP-PEST, enhancing our understanding of its effects on substrate binding and catalytic conformation.

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来源期刊

The Journal of Physical Chemistry B 化学-物理化学

CiteScore

5.80

自引率

9.10%

发文量

965

审稿时长

1.6 months

期刊介绍： An essential criterion for acceptance of research articles in the journal is that they provide new physical insight. Please refer to the New Physical Insights virtual issue on what constitutes new physical insight. Manuscripts that are essentially reporting data or applications of data are, in general, not suitable for publication in JPC B.