1E1U

Human prion protein variant R220K

Summary for 1E1U

• Entry DOI: 10.2210/pdb1e1u/pdb
• Related: 1E1G 1E1J 1E1P 1E1S 1E1W
• NMR Information: BMRB: 4620
• Descriptor: PRION PROTEIN (1 entity in total)
• Functional Keywords: prion protein
• Biological source: HOMO SAPIENS (HUMAN)
• Total number of polymer chains: 1
• Total formula weight: 12531.96

Authors

Calzolai, L.,Lysek, D.A.,Guntert, P.,Von Schroetter, C.,Zahn, R.,Riek, R.,Wuthrich, K. (deposition date: 2000-05-11, release date: 2000-07-20, Last modification date: 2024-11-20)

Primary citation

Calzolai, L.,Lysek, D.A.,Guntert, P.,Von Schroetter, C.,Zahn, R.,Riek, R.,Wuthrich, K.
NMR Structures of Three Single-Residue Variants of the Human Prion Protein
Proc.Natl.Acad.Sci.USA, 97:8340-, 2000

PubMed Abstract: The NMR structures of three single-amino acid variants of the C-terminal domain of the human prion protein, hPrP(121-230), are presented. In hPrP(M166V) and hPrP(R220K) the substitution is with the corresponding residue in murine PrP, and in hPrP(S170N) it is with the corresponding Syrian hamster residue. All three substitutions are in the surface region of the structure of the cellular form of PrP (PrP(C)) that is formed by the C-terminal part of helix 3, with residues 218-230, and a loop of residues 166-172. This molecular region shows high species variability and has been implicated in specific interactions with a so far not further characterized "protein X," and it is related to the species barrier for transmission of prion diseases. As expected, the three variant hPrP(121-230) structures have the same global architecture as the previously determined wild-type bovine, human, murine, and Syrian hamster prion proteins, but with the present study two localized "conformational markers" could be related with single amino acid exchanges. These are the length and quality of definition of helix 3, and the NMR-observability of the residues in the loop 166-172. Poor definition of the C-terminal part of helix 3 is characteristic for murine PrP and has now been observed also for hPrP(R220K), and NMR observation of the complete loop 166-172 has so far been unique for Syrian hamster PrP and is now also documented for hPrP(S170N).

PubMed: 10900000
DOI: 10.1073/PNAS.97.15.8340

Experimental method

SOLUTION NMR