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Insights into Protein-Ligand Interactions in Integrin Complexes: Advances in Structure Determinations.
Journal of Medicinal Chemistry ( IF 7.3 ) Pub Date : 2020-01-30 , DOI: 10.1021/acs.jmedchem.9b01869
Yajun Zheng 1 , Katerina Leftheris 1
Affiliation  

Integrins comprise a family of 24 heterodimeric transmembrane receptors that mediate cell attachment to the extracellular matrix and are critical for cell signaling. There are four classes of integrins: collagen-binding, Arg-Gly-Asp (RGD)-binding, laminin-binding, and leukocyte integrins. Owing to their involvement in modulating various critical cellular processes including proliferation, migration, differentiation, and survival, integrins have been investigated as therapeutic targets. Important progress has been made in the structural elucidation of integrins in recent years. Here we examine the protein–ligand interactions of integrin complexes and the related structure-based drug design of integrin inhibitors. Published integrin structures in the Protein Data Bank (PDB) are examined to gain insights into integrin–ligand interactions as well as the conformational dynamics of integrins.

中文翻译:

整合素复合物中蛋白质-配体相互作用的见解:结构测定的进展。

整联蛋白包含24个异二聚跨膜受体家族,其介导细胞附着于细胞外基质并且对于细胞信号传导至关重要。整联蛋白有四类:胶原蛋白结合,Arg-Gly-Asp(RGD)结合,层粘连蛋白结合和白细胞整联蛋白。由于整合素参与调节各种关键细胞过程,包括增殖,迁移,分化和存活,因此整联蛋白已被研究作为治疗靶标。近年来,在整合素的结构阐明方面已取得重要进展。在这里,我们研究了整联蛋白复合物的蛋白质-配体相互作用以及整联蛋白抑制剂的相关基于结构的药物设计。
更新日期:2020-01-30
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