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Structure-function relationships of the di/tri-peptide transporter of the yeast Saccharomyces cerevisiae:a model system for studying substrate recognition and regulation of membrane proteins involved in peptide transport

机译:酵母酿酒酵母的DI /三肽转运蛋白的结构函数关系:一种研究底物识别的模型系统和肽运输中膜蛋白的调节

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The integral membrane protein Ptr2p transports di/tri-peptides into the yeast S.cerevisiae and is representative of PTR peptide transporters found in all organisms studied to date The power of yeast molecular biology serves to make this system extremely useful as a model for studying the flux of peptides across cellular membranes.The 5~(th)transmembrane domain(TM5)of Ptr2p contains a sequence FYXXINXG('TYING motif)conserved in all PTR family members ranging from yeast to human.Ala-scanning mutagenesis on TM5 was performed to investigate its role in transporter function.
机译:整体膜蛋白PTR2P将DI /三肽传输到酵母S.Cerevisiae中,并且代表在研究酵母分子生物学的所有生物中发现的PTR肽转运蛋白,使该系统非常有用作为研究的模型 PTR2P的5〜(TH)跨膜结构域(TM5)含有序列FYXXINXG('栓基序),在所有PTR家族成员中保守,从酵母到人。扫描诱变对TM5进行扫描诱变 调查其在运输功能中的作用。

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