Detail GPCR Engineering Yields High-Resolution Structural Insights into ß2-Adrenergic Receptor Function   Oleh:  Rosenbaum, Daniel M. ; Cherezov, Vadim ; Hanson, Michael A. ; Rasmussen, Soren G.F. ; Foon, Sun Thian ; Tong, Sun Kobilka ; Hee-Jung, Choi ; Xiao-Jie, Yao ; Weis, William I. ; Stevens, Raymond C. ; Kobilka, Brian K. Jenis: Article from Bulletin/Magazine Dalam koleksi: SCIENCE (keterangan: ada di Proquest) vol. 318 no. 5854 (Nov. 2007), page 1266. Ketersediaan Perpustakaan FK Nomor Panggil: S01.K.2007.09 Non-tandon: 1 (dapat dipinjam: 0) Tandon: tidak ada     Lihat Detail Induk Isi artikel The ß2-adrenergic receptor (ß2AR) is a well-studied prototype for heterotrimeric guanine nucleotide–binding protein (G protein)–coupled receptors (GPCRs) that respond to diffusible hormones and neurotransmitters. To overcome the structural flexibility of the ß2AR and to facilitate its crystallization, we engineered a ß2AR fusion protein in which T4 lysozyme (T4L) replaces most of the third intracellular loop of the GPCR ("ß2AR-T4L") and showed that this protein retains near-native pharmacologic properties. Analysis of adrenergic receptor ligand-binding mutants within the context of the reported high-resolution structure of ß2AR-T4L provides insights into inverse-agonist binding and the structural changes required to accommodate catecholamine agonists. Amino acids known to regulate receptor function are linked through packing interactions and a network of hydrogen bonds, suggesting a conformational pathway from the ligand-binding pocket to regions that interact with G proteins. Opini Anda Klik untuk menuliskan opini Anda tentang koleksi ini! Kembali

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