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dc.contributor.authorLin, Kejiang
dc.contributor.authorLen, Yonggan
dc.contributor.authorFeng, Jao
dc.contributor.authorGao, Hongchang
dc.contributor.authorYou, Qidong
dc.contributor.authorLin, Donghai
dc.contributor.author林东海
dc.contributor.authorLiu, Jingjing
dc.date.accessioned2013-03-28T08:06:31Z
dc.date.available2013-03-28T08:06:31Z
dc.date.issued2012-06
dc.identifier.citationJOURNAL OF PEPTIDE SCIENCE,2012,18(6):413-417zh_CN
dc.identifier.issn1075-2617
dc.identifier.urihttp://dx.doi.org/10.1002/psc.2412
dc.identifier.uriWOS:000304194000008
dc.identifier.urihttps://dspace.xmu.edu.cn/handle/2288/15406
dc.description.abstractWe have previously shown that a recombinant human PTH fragment, Pro-Pro-[Arg11] hPTH (134)-Pro-Pro-Asp (hPTH'), could be a potentially better and more cost-effective therapeutic agent than PTH (134) on osteoporosis. In this report, we characterized the solution conformations of hPTH' by NMR spectroscopy and modeled the interactions between the hPTH' and the PTH receptor. By comparing it with PTH (134) structures and their respective interactions with the PTH receptor, we identified two segments of helix extending from Ile5 to Met8 and from Glu22 to Gln29 with a divided kink between the two helixes around Arg20. Mutated arginine makes hPTH' fill the receptor cavity better as well as forms hydrogen bonds with Val193. Understanding the ligand receptor interactions will help us design small molecules to better mimic the activities of PTH. Copyright (c) 2012 European Peptide Society and John Wiley & Sons, Ltd.zh_CN
dc.description.sponsorshipNatural Science Foundation of China [30730026]; Program of Shanghai Subject Chief Scientist [09XD1405100]zh_CN
dc.language.isoenzh_CN
dc.publisherWILEY-BLACKWELLzh_CN
dc.subjectparathyroid hormonezh_CN
dc.subjectactivityzh_CN
dc.subjectstructurezh_CN
dc.titleStructure of a novel PTH-related peptide hPTH' and its interaction with the PTH receptorzh_CN
dc.typeArticlezh_CN


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