Site-directed mutagenesis demonstrates the plasticity of the beta helix: implications for the structure of the misfolded prion protein.

doi:10.1016/j.str.2009.05.013

Article

Site-directed mutagenesis demonstrates the plasticity of the beta helix: implications for the structure of the misfolded prion protein.

Structure (London, England : 1993) - 15 Jul 2009

Choi Jay H, May Barnaby C H, Govaerts Cedric, Cohen Fred E

Abstract excerpt

The left-handed parallel beta helix (LbetaH) fold has recently received attention as a possible structure for the prion protein (PrP) in its misfolded state. In light of this interest, we have developed an experimental system to examine the structural requirements of the LbetaH fold, using a known LbetaH protein, UDP-N-acetylglucosamine acyltransferase (LpxA), from E. coli. We showed that the beta helix can...

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Site-directed mutagenesis demonstrates the plasticity of the beta helix: implications for the structure of the misfolded prion protein.

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