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首页> 外文会议>International Peptide Symposium;European Peptide Symposium >Biochemical and mutagenic analysis of a G protein-coupled receptor:Photocrosslinking of the tridecapeptide alpha-Factor into Ste2p of Saccharomyces cerevisiae reveals contact points between the peptide and its receptor binding site
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Biochemical and mutagenic analysis of a G protein-coupled receptor:Photocrosslinking of the tridecapeptide alpha-Factor into Ste2p of Saccharomyces cerevisiae reveals contact points between the peptide and its receptor binding site

机译：G蛋白偶联受体的生化和致突变分析：Trideacapeptideα-Temo酿酒酵母群STE2P的光源瘤揭示肽及其受体结合位点之间的接触点

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摘要

Understanding the biologically active structure of a peptide hormone is an important step in the development of agonists and antagonists for its receptor.The most direct approach toward this end would be the determination of an X-ray or high resolution NMR structure of the peptide-receptor complex.To date such data has been obtained only for a few ligands bound to G protein-coupled receptors(GPCRs).Other strategies are needed to gain evidence for the bound structure.Among indirect routes,photocross-linking coupled with site-directed mutagenesis yields contact points between peptide side chains and residues in the receptor.This information can be used to dock the peptide into the receptor and thereby infer its biologically active structure.We have used photocross-linking of iodinated analogs of the alpha-factor(WHWLQLKPGQPMY)of Saccharomyces cerevisiae to determine interactions of residues of this mating pheromone with its G protein-coupled receptor(Ste2p).Here we discuss the use of biotinylated ligands to assess peptide-receptor contacts.
机译：了解肽激素的生物活性结构是对其受体发育激动剂和拮抗剂的重要一步。最直接的方法朝向该目的是肽受体的X射线或高分辨率NMR结构的测定迄今为止，仅针对G蛋白偶联受体（GPCR）的少数配体获得了这种数据。需要策略来获得界定结构的证据.AMONG间接路线，光源联系与点定向诱变相结合产生肽侧链和受体中残基之间的接触点。该信息可用于将肽停靠到受体中，从而推断其生物活性结构。我们使用了α-因子（Whwlqlkpgqpmy）的碘化类似物的光源连接酿酒酵母中的酿酒酵母与其与其G蛋白偶联受体（STE2P）的与其合并信息素的残留物相互作用。我们讨论了生物的使用锡氧化的配体评估肽受体接触。

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