Protein disulfide isomerases exploit synergy between catalytic and specific binding domains
نویسندگان
چکیده
منابع مشابه
Protein disulfide isomerases exploit synergy between catalytic and specific binding domains.
Protein disulfide isomerases (PDIs) catalyse the formation of native disulfide bonds in protein folding pathways. The key steps involve disulfide formation and isomerization in compact folding intermediates. The high-resolution structures of the a and b domains of PDI are now known, and the overall domain architecture of PDI and its homologues can be inferred. The isolated a and a' domains of P...
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ژورنال
عنوان ژورنال: EMBO reports
سال: 2002
ISSN: 1469-221X,1469-3178
DOI: 10.1093/embo-reports/kvf035