2L40
Mouse prion protein (121-231) containing the substitution Y169A
Summary for 2L40
| Entry DOI | 10.2210/pdb2l40/pdb |
| Related | 2L1D 2L1E 2L1H 2L1K 2L39 |
| NMR Information | BMRB: 17213 |
| Descriptor | Major prion protein (1 entity in total) |
| Functional Keywords | prion, mutation, membrane protein, prp |
| Biological source | Mus musculus (mouse) |
| Total number of polymer chains | 1 |
| Total formula weight | 13316.78 |
| Authors | Christen, B.,Damberger, F.F.,Perez, D.R.,Hornemann, S.,Wuthrich, K. (deposition date: 2010-09-28, release date: 2011-08-10, Last modification date: 2023-06-14) |
| Primary citation | Damberger, F.F.,Christen, B.,Perez, D.R.,Hornemann, S.,Wuthrich, K. Cellular prion protein conformation and function. Proc.Natl.Acad.Sci.USA, 108:17308-17313, 2011 Cited by PubMed Abstract: In the otherwise highly conserved NMR structures of cellular prion proteins (PrP(C)) from different mammals, species variations in a surface epitope that includes a loop linking a β-strand, β2, with a helix, α2, are associated with NMR manifestations of a dynamic equilibrium between locally different conformations. Here, it is shown that this local dynamic conformational polymorphism in mouse PrP(C) is eliminated through exchange of Tyr169 by Ala or Gly, but is preserved after exchange of Tyr 169 with Phe. NMR structure determinations of designed variants of mouse PrP(121-231) at 20 °C and of wild-type mPrP(121-231) at 37 °C together with analysis of exchange effects on NMR signals then resulted in the identification of the two limiting structures involved in this local conformational exchange in wild-type mouse PrP(C), and showed that the two exchanging structures present characteristically different solvent-exposed epitopes near the β2-α2 loop. The structural data presented in this paper provided a platform for currently ongoing, rationally designed experiments with transgenic laboratory animals for renewed attempts to unravel the so far elusive physiological function of the cellular prion protein. PubMed: 21987789DOI: 10.1073/pnas.1106325108 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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