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  • Title: Synthetic human prion protein octapeptide repeat binds to the proteinase K active site.
    Author: Georgieva D, Rypniewski W, Echner H, Perbandt M, Koker M, Clos J, Redecke L, Bredehorst R, Voelter W, Genov N, Betzel C.
    Journal: Biochem Biophys Res Commun; 2004 Dec 24; 325(4):1406-11. PubMed ID: 15555583.
    Abstract:
    Proteinase K is widely used in tests for the presence of infectious prion protein causing fatal spongiform encephalopathies. To investigate possible interactions between the enzyme and the functionally important N-terminal prion domain, we crystallized mercury-inhibited proteinase K in the presence of the synthetic peptides GGGWGQPH and HGGGW. The octapeptide sequence is identical to that of a single octapeptide repeat (OPR) from the physiologically important OPR region. Here, we present the first direct evidence for the complex formation between a proteolytic enzyme and a segment of human prion molecule. The X-ray structures of the complexes at 1.4 and 1.8A resolution, respectively, revealed that in both cases the segment GGG is strongly bound as a real substrate at the substrate recognition site of the proteinase forming an antiparallel beta-strand between the two parallel strands of Asn99-Tyr104 and Ser132-Gly136. The complex is stabilized through an extended H-bonding network.
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