Human transforming growth factor β type I receptor in complex with kinase inhibitor SB505124.

IF 1.1 4区生物学 Q4 BIOCHEMICAL RESEARCH METHODS

Acta crystallographica. Section F, Structural biology communications Pub Date : 2024-11-01 Epub Date: 2024-10-23 DOI:10.1107/S2053230X24010094

Jhon A Rodriguez Buitrago, Maréne Landström, Magnus Wolf-Watz

引用次数: 0

Abstract

The crystal structure of the intracellular domain of transforming growth factor β type I receptor (TβR1) in complex with the competitive inhibitor SB505124 is presented. The study provides insights into the structure and function of TβR1 in complex with SB505124, and as such offers molecular-level understanding of the inhibition of this critical signalling pathway. The potential of SB505124 as an avenue for therapy in cancer treatment is discussed on basis of the results.

查看原文本刊更多论文

人转化生长因子 β I 型受体与激酶抑制剂 SB505124 的复合物。

该研究展示了转化生长因子β I型受体（TβR1）胞内结构域与竞争性抑制剂SB505124复合物的晶体结构。该研究深入揭示了 TβR1 与 SB505124 复合物的结构和功能，从而提供了对抑制这一关键信号通路的分子水平的理解。在此基础上讨论了 SB505124 作为癌症治疗途径的潜力。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

求助全文

约1分钟内获得全文求助全文

来源期刊

Acta crystallographica. Section F, Structural biology communications BIOCHEMICAL RESEARCH METHODSBIOCHEMISTRY &-BIOCHEMISTRY & MOLECULAR BIOLOGY

CiteScore

1.90

自引率

0.00%

发文量

期刊介绍： Acta Crystallographica Section F is a rapid structural biology communications journal. Articles on any aspect of structural biology, including structures determined using high-throughput methods or from iterative studies such as those used in the pharmaceutical industry, are welcomed by the journal. The journal offers the option of open access, and all communications benefit from unlimited free use of colour illustrations and no page charges. Authors are encouraged to submit multimedia content for publication with their articles. Acta Cryst. F has a dedicated online tool called publBio that is designed to make the preparation and submission of articles easier for authors.