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1E1P

Human prion protein variant S170N

1E1P の概要
エントリーDOI10.2210/pdb1e1p/pdb
関連するPDBエントリー1E1G 1E1J 1E1S 1E1U 1E1W
分子名称PRION PROTEIN (1 entity in total)
機能のキーワードprion protein
由来する生物種HOMO SAPIENS (HUMAN)
タンパク質・核酸の鎖数1
化学式量合計12587.00
構造登録者
Calzolai, L.,Lysek, D.A.,Guntert, P.,Von Schroetter, C.,Zahn, R.,Riek, R.,Wuthrich, K. (登録日: 2000-05-09, 公開日: 2000-07-20, 最終更新日: 2011-07-13)
主引用文献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
Cited by
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
主引用文献が同じPDBエントリー
実験手法
SOLUTION NMR
構造検証レポート
Validation report summary of 1e1p
検証レポート(詳細版)ダウンロードをダウンロード

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件を2024-10-30に公開中

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