Binding of fluorinated phenylalanine alpha-factor analogues to Ste2p: evidence for a cation-pi binding interaction between a peptide ligand and its cognate G protein-coupled receptor.
Binding of fluorinated phenylalanine alpha-factor analogues to Ste2p: evidence for a cation-pi binding interaction between a peptide ligand and its cognate G protein-coupled receptor.
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氟化苯丙氨酸 α 因子类似物与 Ste2p 的结合：肽配体与其同源 G 蛋白偶联受体之间阳离子-π 结合相互作用的证据。
DOI：
10.1021/bi100280f
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发表时间：
2010
期刊：
影响因子：
2.9
通讯作者：
Naider,Fred
中科院分区：
文献类型：
--
作者：
Tantry,Subramanyam;Ding,Fa-Xiang;Dumont,Mark;Becker,JeffreyM;Naider,Fred
Ste2p, a G protein-coupled receptor (GPCR), binds α-factor, WHWLQLKPGQPMY, a tridecapeptide pheromone secreted by yeast cells. Upon α-factor binding, Ste2p undergoes conformational changes activating a signal transduction system through its associated heterotrimeric G protein leading to the arrest of cell growth in the G1 phase to prepare cells for mating. Previous studies have indicated that Tyr at position 13 of α-factor interacts with Arg58 on transmembrane one (TM1) of Ste2p. This observation prompted this investigation to determine whether a cation−π type of interaction occurred between these residues. Tyrosine at position 13 of α-factor was systematically substituted with analogous amino acids with varying cation−π binding energies using solid-phase peptide synthesis, and these analogues were modified by derivatization of their Lys7residue with the fluorescent group 7-nitrobenz-2-oxa-1,3-diazole (NBD) to serve as a useful probe for binding determination. Saturation binding of these peptides to Ste2p was assayed using whole yeast cells and a flow cytometer. In parallel the biological activities of the peptides were determined using a growth arrest assay. The data provide evidence for the presence of a cation−π interaction between Arg58 of Ste2p and Tyr13of α-factor.
