核磁共振解决人类朊蛋白的结构。
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锥盘R,刘,Luhrs T里克•R•冯•Schroetter C,洛佩兹加西亚F,钢坯M, Calzolai L G,伍斯里奇K
核磁共振解决人类朊蛋白的结构。
《美国国家科学院刊S a . 2000年1月4,97 (1):145 - 50。
- PubMed ID
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10618385 (在PubMed]
- 文摘
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人类朊蛋白的核磁共振结构重组,hPrP(23 - 230),和两个c端片段,hPrP(90 - 230)和hPrP(121 - 230),包括一个球状域从残留125 - 228年的详细结构,和一个氨基端灵活无序的“尾巴”。The globular domain contains three alpha-helices comprising the residues 144-154, 173-194, and 200-228 and a short anti-parallel beta-sheet comprising the residues 128-131 and 161-164. Within the globular domain, three polypeptide segments show increased structural disorder: i.e., a loop of residues 167-171, the residues 187-194 at the end of helix 2, and the residues 219-228 in the C-terminal part of helix 3. The local conformational state of the polypeptide segments 187-193 in helix 2 and 219-226 in helix 3 is measurably influenced by the length of the N-terminal tail, with the helical states being most highly populated in hPrP(23-230). When compared with the previously reported structures of the murine and Syrian hamster prion proteins, the length of helix 3 coincides more closely with that in the Syrian hamster protein whereas the disordered loop 167-171 is shared with murine PrP. These species variations of local structure are in a surface area of the cellular form of PrP that has previously been implicated in intermolecular interactions related both to the species barrier for infectious transmission of prion disease and to immune reactions.