Motion in Proteinaceous Infectious Particles (Prions) [prion]

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Classification Suspected Domain Motion, Unclassifiable Mechanism [D-?-1]

Structures 1AG2 Conformation 1 [ PartsList ]

Description NMR studies by Donne et al. (1997) conclude that Hamster PrP is a remarkably flexible molecule in the 29-124 region. This flexibility is related to its pathogenic properties, providing a lower energy barrier between the PrP and PrSC conformations than would be expected for a typical protein. Donne et al. speculate that this flexibility may also be related to its normal function in vivo.

Particular values describing motion Experimental Methods = nci (NMR, CD, and FTIR) Creation Date = 19971227 Modification Date = 19971227 Location of a Hinge (residue selection) = 29-124 (flexible region)

References Donne DG, Viles JH, Groth D, Mehlhorn I, James TL, Cohen FE, Prusiner SB, Wright PE, Dyson HJ (1997). Structure of the recombinant full-length hamster prion protein PrP(29-231): the N terminus is highly flexible. Pro.c Natl. Acad. Sci. U.S.A.:94(25):13452-13457. [Medline info for 94278498]

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Copyright 1995-2005 M. Gerstein, W. Krebs, S. Flores, N. Echols, and others
Email: Mark.Gerstein _at_ yale.edu