1h0l

HUMAN PRION PROTEIN 121-230 M166C/E221CHUMAN PRION PROTEIN 121-230 M166C/E221C

Structural highlights 1h0l is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1fkc, 1fo7, 1i4m, 1qlx, 1qlz, 1qm0, 1qm1, 1qm2, 1qm3 Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. NMR structure of a variant human prion protein with two disulfide bridges.,Zahn R, Guntert P, von Schroetter C, Wuthrich K J Mol Biol. 2003 Feb 7;326(1):225-34. PMID:12547204 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Doppel Prion

spinqualitylabelsall models 1h0l, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image