1H0L

HUMAN PRION PROTEIN 121-230 M166C/E221C

Summary for 1H0L

• Entry DOI: 10.2210/pdb1h0l/pdb
• Related: 1FKC 1FO7 1I4M 1QLX 1QLZ 1QM0 1QM1 1QM2 1QM3
• Descriptor: MAJOR PRION PROTEIN (1 entity in total)
• Functional Keywords: cell cycle, brain, glycoprotein, gpi-anchor, polymorphism, disease mutation
• Biological source: HOMO SAPIENS (HUMAN)
• Cellular location: Cell membrane; Lipid-anchor, GPI-anchor. Isoform 2: Cytoplasm: P04156
• Total number of polymer chains: 1
• Total formula weight: 13106.57

Authors

Zahn, R.,Guntert, P.,Wuthrich, K. (deposition date: 2002-06-24, release date: 2003-01-30, Last modification date: 2024-10-23)

Primary citation

Zahn, R.,Guntert, P.,Von Schroetter, C.,Wuthrich, K.
NMR Structure of a Variant Human Prion Protein with Two Disulfide Bridges
J.Mol.Biol., 326:225-, 2003

PubMed Abstract: The nuclear magnetic resonance structure of the globular domain with residues 121-230 of a variant human prion protein with two disulfide bonds, hPrP(M166C/E221C), shows the same global fold as wild-type hPrP(121-230). It contains three alpha-helices of residues 144-154, 173-194 and 200-228, an anti-parallel beta-sheet of residues 128-131 and 161-164, and the disulfides Cys166-Cys221 and Cys179-Cys214. The engineered extra disulfide bond in the presumed "protein X"-binding site is accommodated with slight, strictly localized conformational changes. High compatibility of hPrP with insertion of a second disulfide bridge in the protein X epitope was further substantiated by model calculations with additional variant structures. The ease with which the hPrP structure can accommodate a variety of locations for a second disulfide bond within the presumed protein X-binding epitope suggests a functional role for the extensive perturbation by a natural second disulfide bond of the corresponding region in the human doppel protein.

PubMed: 12547204
DOI: 10.1016/S0022-2836(02)01332-3

Experimental method

SOLUTION NMR