Issue October 2011
Volume 29No. 2 (p 251-423) October 2011 ISSN 0739-1102 The Structural Stability of Wild-type Horse Prion ProteinPrion diseases (e.g. Creutzfeldt-Jakob disease (CJD), variant CJD (vCJD), Gerstmann-Sträussler-Scheinker syndrome (GSS), Fatal Familial Insomnia (FFI) and Kuru in humans, scrapie in sheep, bovine spongiform encephalopathy (BSE or ‘mad-cow’ disease) and chronic wasting disease (CWD) in cattles) are invariably fatal and highly infectious neurodegenerative diseases affecting humans and animals. However, by now there have not been some effective therapeutic approaches or medications to treat all these prion diseases. Rabbits, dogs, and horses are the only mammalian species reported to be resistant to infection from prion
diseases isolated from other species. Recently, the β2-α2 loop has been reported to contribute to their protein structural stabilities. The author has found that rabbit prion protein has a strong salt bridge ASP177-ARG163 (like a taut bow string) keeping this loop linked. This paper confirms that this salt bridge also contributes to the structural stability of horse prion protein. Thus, the region of β2-α2 loop might be a potential drug target region. Besides this very important salt bridge, other four important salt bridges GLU196-ARG156-HIS187, ARG156-ASP202
and GLU211-HIS177 are also found to greatly contribute to the structural stability of horse prion protein. Rich databases of salt bridges, hydrogen bonds and hydrophobic contacts for horse prion protein can be found in this paper.
Key words: Prion diseases; Immunity; Horse, Rabbit and dog prion proteins; Molecular dynamics. This article can be cited as: Jiapu Zhang. The Structural Stability of Wild-type Horse Prion Protein J. Biomol Struct Dyn 29(2)369-377 (2011). Jiapu Zhang School of Sciences, Information
Technology and Engineering,
University of Ballarat, Mount Helen,
Ballarat, Victoria 3353, Australia Supplementary Materials Videos 1-2 In Fig. 4, the important salt bridges of initial structure of HoPrPC (i.e. 2KU4.pdb) are illuminated. Videos 1-2 illuminate the structural dynamics of all these important salt bridges during the whole 30 ns’ simulations. Video 1 is for seed1 and Video 2 is for seed2. For each video, there are 150 frames and there are 5 frames (at the snapshots of 200 ps, 400 ps, 600 ps, 800 ps, 1000 ps) taken for each MD nanosecond. Videos 1-2 are movies of 6 real time seconds, thus in each real time 1 second, 5 nanoseconds of 25 MD frames are shown. Table 1 is the database of the Hydrogen Bonds of horse prion protein under low pH environment at 350 K for both seed1 and seed2. The detailed descriptions for Tables 1-3 can be found at the header of each database. download table1.pdf Table 2 is the database of the Hydrophobic Bonds of horse prion protein under low pH environment at 350 K for both seed1 and seed2. download table2.pdf Table 3 is the database of Salt Bridges of horse prion protein at 300K for both seed1 and seed2, under neutral pH environment. These three rich databases of Salt Bridges, Hydrophobic and Hydrogen Bonds of horse prion protein should present very useful structural bioinformatics to study horse prion protein and prion diseases. download table3.pdf Subscription is more cost effective than purchasing PDFs on-the-fly. Click here for details. |
|
Member Login | Home | Subscribe | Cancer Watch | Cancer Technologies | Editorial Officers | Instructions | Editor-in-Chief | Contact Us
Adenine Press, 2066 Central Avenue, Schenectady, NY 12304 USA |
Re-initialize IP-based Login |
