The PrP-like Protein Doppel Binds Copper
نویسندگان
چکیده
منابع مشابه
A pathogenic PrP mutation and doppel interfere with polarized sorting of the prion protein.
Several proteins linked to neurodegenerative diseases, such as the beta-amyloid precursor protein, amyloid beta-peptide, beta-secretase, and tau, undergo selective polarized sorting. We investigated polarized sorting of the mammalian prion protein (PrP(C)) and its homologue doppel (Dpl). In contrast to Dpl, which accumulates on the apical surface, PrP(C) is targeted selectively to the basolater...
متن کاملNeurobiology of Disease Truncated Prion Protein and Doppel Are Myelinotoxic in the Absence of Oligodendrocytic PrP
The cellular prion protein PrP C confers susceptibility to transmissible spongiform encephalopathies, yet its normal function is unknown. Although PrP -deficient mice develop and live normally, expression of amino proximally truncated PrP C ( PrP) or of its structural homolog Doppel (Dpl) causes cerebellar degeneration that is prevented by coexpression of full-length PrP . We now report that mi...
متن کاملTargeting prion-like protein doppel selectively suppresses tumor angiogenesis.
Controlled and site-specific regulation of growth factor signaling remains a major challenge for current antiangiogenic therapies, as these antiangiogenic agents target normal vasculature as well tumor vasculature. In this article, we identified the prion-like protein doppel as a potential therapeutic target for tumor angiogenesis. We investigated the interactions between doppel and VEGFR2 and ...
متن کاملNMR structure of the human doppel protein.
The NMR structure of the recombinant human doppel protein, hDpl(24-152), contains a flexibly disordered "tail" comprising residues 24-51, and a globular domain extending from residues 52 to 149 for which a detailed structure was obtained. The globular domain contains four alpha-helices comprising residues 72-80 (alpha1), 101-115 (alpha2(a)), 117-121 (alpha2(b)), and 127-141 (alpha3), and a shor...
متن کاملStability and conformational properties of doppel, a prion-like protein, and its single-disulphide mutant.
Both prion protein and the structurally homologous protein doppel are associated with neurodegenerative disease by mechanisms which remain elusive. We have prepared murine doppel, and a mutant with one of the two disulphide bonds removed, in the expectation of increasing the similarity of doppel to prion protein in terms of conformation and stability. Unfolding studies of doppel and the mutant ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2003
ISSN: 0021-9258
DOI: 10.1074/jbc.m210875200