Laboratory of Chemical Biology and Signal Transduction, The Rockefeller University , 1230 York Avenue, New York , New York 10065, United States.
Biochemistry. 2013 Dec 3;52(48):8625-32. doi: 10.1021/bi401300y. Epub 2013 Nov 19.
It has been 50 years since F. H. Westheimer and colleagues reported the first use of a photoactivatable cross-linking reagent to study the active site of chymotrypsin. In studies of seven transmembrane helical receptors, also known as G protein-coupled receptors (GPCRs), recent simultaneous advances in structural biology, molecular dynamics simulations, and amber codon suppression methods have allowed the development of a targeted photo-cross-linking strategy to probe receptor-ligand interactions in cell membranes. We review here recent advances in targeted photo-cross-linking of GPCR-ligand complexes in the context of extensive earlier work that primarily relied upon the use of ligand analogues with photoactivatable constituents.
自 F. H. Westheimer 和同事报道首次使用光活化交联试剂研究糜蛋白酶活性位点以来，已经过去了 50 年。在对七跨膜螺旋受体（也称为 G 蛋白偶联受体（GPCR））的研究中，结构生物学、分子动力学模拟和琥珀酰氨-色氨酸突变抑制方法的最新同步进展，使得靶向光交联策略得以发展，以在细胞膜中探测受体-配体相互作用。我们在这里回顾了在广泛的早期工作的基础上，主要依赖于使用带有光活化成分的配体类似物的情况下，GPCR-配体复合物的靶向光交联的最新进展。
