About: Conformational changes in redox pairs of protein structures

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An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Conformational changes in redox pairs of protein structures
Creator	Fan, Samuel Feng, Lina George, Richard Haworth, Naomi Liu, Jason Wouters, Merridee
Source	Medline; PMC
abstract	Disulfides are conventionally viewed as structurally stabilizing elements in proteins but emerging evidence suggests two disulfide subproteomes exist. One group mediates the well known role of structural stabilization. A second redox-active group are best known for their catalytic functions but are increasingly being recognized for their roles in regulation of protein function. Redox-active disulfides are, by their very nature, more susceptible to reduction than structural disulfides; and conversely, the Cys pairs that form them are more susceptible to oxidation. In this study, we searched for potentially redox-active Cys Pairs by scanning the Protein Data Bank for structures of proteins in alternate redox states. The PDB contains over 1134 unique redox pairs of proteins, many of which exhibit conformational differences between alternate redox states. Several classes of structural changes were observed, proteins that exhibit: disulfide oxidation following expulsion of metals such as zinc; major reorganisation of the polypeptide backbone in association with disulfide redox-activity; order/disorder transitions; and changes in quaternary structure. Based on evidence gathered supporting disulfide redox activity, we propose disulfides present in alternate redox states are likely to have physiologically relevant redox activity.
has issue date	2009-08-01(xsd:dateTime)
bibo:doi	10.1002/pro.175
bibo:pmid	19598234
has license	green-oa
sha1sum (hex)	ec74db66f65c0201ea511463f4b67fde387eafe5
schema:url	https://doi.org/10.1002/pro.175
resource representing a document's title	Conformational changes in redox pairs of protein structures
has PubMed Central identifier	PMC2776962
has PubMed identifier	19598234
schema:publication	Protein Science
resource representing a document's body	covid:ec74db66f65c0201ea511463f4b67fde387eafe5#body_text
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