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- W2600256199 abstract "Vicinal disulfides between sequence-adjacent cysteine residues are very rare and rather startling structural features which play a variety of functional roles. Typically discussed as an isolated curiosity, they have never received a general treatment covering both cis and trans forms. Enabled by the growing database of high-resolution structures, required deposition of diffraction data, and improved methods for discriminating reliable from dubious cases, we identify and describe distinct protein families with reliably genuine examples of cis or trans vicinal disulfides and discuss their conformations, conservation, and functions. No cis-trans interconversions and only one case of catalytic redox function are seen. Some vicinal disulfides are essential to large, functionally coupled motions, whereas most form the centers of tightly packed internal regions. Their most widespread biological role is providing a rigid hydrophobic contact surface under the undecorated side of a sugar or multiring ligand, contributing an important aspect of binding specificity." @default.
- W2600256199 created "2017-04-07" @default.
- W2600256199 creator A5008253607 @default.
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- W2600256199 creator A5088973528 @default.
- W2600256199 date "2017-05-01" @default.
- W2600256199 modified "2023-10-16" @default.
- W2600256199 title "Broad Analysis of Vicinal Disulfides: Occurrences, Conformations with Cis or with Trans Peptides, and Functional Roles Including Sugar Binding" @default.
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- W2600256199 doi "https://doi.org/10.1016/j.jmb.2017.03.017" @default.
- W2600256199 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5500257" @default.
- W2600256199 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/28336403" @default.
- W2600256199 hasPublicationYear "2017" @default.
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