Prion protein NMR structures of chickens, turtles, and frogs

被引:150
作者
Calzolai, L
Lysek, DA
Pérez, DR
Güntert, P
Wüthrich, K
机构
[1] ETH, Inst Molekularbiol & Biophys, CH-8093 Zurich, Switzerland
[2] Univ Chile, Fac Ciencias, Grad Program Mol Cellular & Neurosci Biol, Santiago, Chile
关键词
nonmammalian species; transmissible spongiform encephalopathy;
D O I
10.1073/pnas.0408939102
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
The NMR structures of the recombinant prion proteins from chicken (Gallus gallus; chPrP), the red-eared slider turtle (Trachemys scripta; tPrP), and the African clawed frog (Xenopus laevis; xlPrP) are presented. The amino acid sequences of these prion proteins show approximate to30% identity with mammalian prion proteins. All three species form the same molecular architecture as mammalian PrPc, with a long, flexibly disordered tail attached to the N-terminal end of a globular domain. The globular domain in chPrP and tPrP contains three alpha-helices, one short 3(10)-helix, and a short antiparallel beta-sheet. In xlPrP, the globular domain includes three alpha-helices and a somewhat longer p-sheet than in the other species. The spatial arrangement of these regular secondary structures coincides closely with that of the globular domain in mammalian prion proteins. Based on the low sequence identity to mammalian PrPs, comparison of chPrP, tPrP, and xIPrP with mammalian PrPc structures is used to identify a set of essential amino acid positions for the preservation of the same PrPc fold in birds, reptiles, amphibians, and mammals. There are additional conserved residues without apparent structural roles, which are of interest for the ongoing search for physiological functions of PrPc in healthy organisms.
引用
收藏
页码:651 / 655
页数:5
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