1u3m

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NMR structure of the chicken prion protein fragment 128-242

Overview

The NMR structures of the recombinant prion proteins from chicken (Gallus, gallus; chPrP), the red-eared slider turtle (Trachemys scripta; tPrP), and, the African clawed frog (Xenopus laevis; xlPrP) are presented. The amino, acid sequences of these prion proteins show approximately 30% identity, with mammalian prion proteins. All three species form the same molecular, architecture as mammalian PrPC, with a long, flexibly disordered tail, attached to the N-terminal end of a globular domain. The globular domain, in chPrP and tPrP contains three alpha-helices, one short 3(10)-helix, and, a short antiparallel beta-sheet. In xlPrP, the globular domain includes, three alpha-helices and a somewhat longer beta-sheet than in the other, species. The spatial arrangement of these regular secondary structures, coincides closely with that of the globular domain in mammalian prion, proteins. Based on the low sequence identity to mammalian PrPs, comparison, of chPrP, tPrP, and xlPrP with mammalian PrPC structures is used to, identify a set of essential amino acid positions for the preservation of, the same PrPC fold in birds, reptiles, amphibians, and mammals. There are, additional conserved residues without apparent structural roles, which are, of interest for the ongoing search for physiological functions of PrPC in, healthy organisms.

About this Structure

1U3M is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.

Reference

Prion protein NMR structures of chickens, turtles, and frogs., Calzolai L, Lysek DA, Perez DR, Guntert P, Wuthrich K, Proc Natl Acad Sci U S A. 2005 Jan 18;102(3):651-5. Epub 2005 Jan 12. PMID:15647366

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