Structural mechanism of disulphide bond-mediated redox switches
نویسندگان
چکیده
منابع مشابه
Structural mechanism of disulphide bond - mediated redox
The oxidation of cysteine sulphydryl in proteins produces sulphenic acid that can form a reversible disulphide bond with another cysteine. The disulphide bond formation often triggers switches in protein structure and activity, especially when the distance between the two cysteine sulphur atoms is longer than the resulting disulphide bond distance. As an early example for the reversible disulph...
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The formation of protein disulphide bonds in newly synthesised secretory proteins within the endoplasmic reticulum (ER) depends on an electron transfer system in which oxidising equivalents are passed from molecular oxygen through several carriers within the oxidase Ero1 to protein disulphide isomerase (PDI) and then to the reduced protein substrate. Recent articles published in The EMBO Journa...
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The formation of disulphide bridges among cysteines is an important feature of protein structures. Here we develop new methods for the prediction of disulphide bond connectivity. We first build a large curated data set of proteins containing disulphide bridges and then use 2-Dimensional Recursive Neural Networks to predict bonding probabilities between cysteine pairs. These probabilities in tur...
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The presence and location of intramolecular disulphide bonds are a key determinant of the structure and function of proteins. Intramolecular disulphide bonds in proteins have previously been analyzed under the assumption that there is no clear relationship between disulphide arrangement and disulphide concentration. To investigate this, a set of sequence nonhomologous protein chains containing ...
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Redox regulation of chloroplast enzymes via disulphide reduction is believed to control the rates of CO2 fixation. The study of the thioredoxin reduction pathways and of various target enzymes lead to the following guidelines.
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ژورنال
عنوان ژورنال: Journal of Biochemistry
سال: 2012
ISSN: 0021-924X
DOI: 10.1093/jb/mvs046