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자료유형
학술저널
저자정보
저널정보
대한생화학·분자생물학회 Experimental and Molecular Medicine Experimental and Molecular Medicine 제39권 제6호
발행연도
2007.1
수록면
769 - 777 (9page)

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Prion proteins (PrPs) are infectious pathogens that cause a group of invariably fatal, neurodegenerative diseases, including Creutzfeldt-Jakob disease, by duced by various species, including reptile, rodent, ru-minant and mammals, during normal metabolic pro-cesses, but they can be slowly changed into patho-genic isoforms upon contact with other infectious PrP isoforms. This transmision can occur acros species bariers. In the present study, phylogram for each PrP sequence was generated by PAUP* 4.0 program using Neighbor-Joining method with 1,000 times boot-strapping process for the phylogenetic analysis. The by the SANDER module in the AMBER 7 package using Amber 99 force field. Al the simulation process was conducted in the IBM p690 Supercomputing System in Korea Institute of Science and Technology Informa-tion. To reduce the calculation time, we used ‘the Generalized Born (GB) model'. We compared the se-quences and structural characteristics of normal and pathogenic (E200K) human PrPs with those of other reptile, rodent, ruminant and mamalian PrPs. Phylo-sequence is the most distinct of the PrPs analyzed, it nonetheless retains five conserved secondary struc-tural elements that are similar to those found in the mammalian PrPs, suggesting that these elements have important functions in vivo. The RMS deviation between the normal and E200K human PrPs was larger than that between the normal human and bovine PrPs, and all of the β-sheet structures in human E200K PrP were very stable during MD simulations.

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