Redox-dependent domain rearrangement of protein disulfide isomerase coupled with exposure of its substrate-binding hydrophobic surface

Journal of Molecular Biology

Volumn 396, Issue 2, 2010, Pages 361-374

  Serve, Olivier ^a,b,c   Kamiya, Yukiko ^a,b,c   Maeno, Aya ^b   Nakano, Michiko ^b,c   Murakami, Chiho ^b   Sasakawa, Hiroaki ^b,c   Yamaguchi, Yoshiki ^b,d   Harada, Takushi ^b   Kurimoto, Eiji ^b   Yagi Utsumi, Maho ^b   Iguchi, Takeshi ^e   Inaba, Kenji ^f   Kikuchi, Jun ^g   Asami, Osamu ^h   Kajino, Tsutomu ^h   Oka, Toshihiko ⁱ   Nakasako, Masayoshi ^i,j   Kato, Koichi ^a,b,c  

^a OKAZAKI INSTITUTE FOR INTEGRATIVE BIOSCIENCE   (Japan)

^b NAGOYA CITY UNIVERSITY   (Japan)

^c INSTITUTE FOR MOLECULAR SCIENCE   (Japan)

^d RIKEN   (Japan)

^e Fujiya Co Ltd   (Japan)

^f KYUSHU UNIVERSITY   (Japan)

^g RIKEN Center for Sustainable Resource Science   (Japan)

^h Rd Management Section   (Japan)

ⁱ KEIO UNIVERSITY   (Japan)

^j RIKEN HARIMA INSTITUTE   (Japan)

more..

Author keywords

Domain rearrangement; Molecular chaperone; NMR; Protein disulfide isomerase; SAXS

Indexed keywords

CHAPERONE; PROTEIN DISULFIDE ISOMERASE; SOLVENT;

ARTICLE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; DEUTERIUM HYDROGEN EXCHANGE; DISULFIDE BOND; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME BINDING; ENZYME SUBSTRATE; FUNGUS; HYDROPHOBICITY; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; OXIDATION REDUCTION REACTION; OXIDATION REDUCTION STATE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; THERMOPHILE; X RAY CRYSTALLOGRAPHY; ASCOMYCETES; BINDING SITE; BIOLOGICAL MODEL; CHEMICAL STRUCTURE; CHEMISTRY; ENZYMOLOGY; METABOLISM; PHYSIOLOGY; PROTEIN TERTIARY STRUCTURE; SMALL ANGLE SCATTERING; X RAY DIFFRACTION;

FUNGI; HUMICOLA INSOLENS;

ASCOMYCOTA; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; HYDROPHOBICITY; MODELS, BIOLOGICAL; MODELS, MOLECULAR; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; OXIDATION-REDUCTION; PROTEIN DISULFIDE-ISOMERASES; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; SCATTERING, SMALL ANGLE; X-RAY DIFFRACTION;

EID: 77449149046     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2009.11.049     Document Type: Article

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