Research ArticleProtein Motifs

Protein folding creates structure-based, noncontiguous consensus phosphorylation motifs recognized by kinases

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Science Signaling  04 Nov 2014:
Vol. 7, Issue 350, pp. ra105
DOI: 10.1126/scisignal.2005412

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Origami-Like Substrate Recognition

Proteins fold into complex three-dimensional structures, yet most sites in proteins that are modified posttranslationally have been identified within short linear consensus motifs in the primary amino acid sequence. Duarte et al. found that kinases can recognize a consensus site that is formed by distinct noncontiguous parts of the folded substrate protein. They characterized in α-tubulin an example of what they termed a “structurally formed” consensus site, a threonine residue phosphorylated by a specific member of the protein kinase C (PKC) family, and then identified structurally formed consensus sites in other substrates of PKC and PKA (protein kinase A). Thus, researchers need to look beyond the linear sequence of the protein to its three-dimensional structure to identify all of the potential consensus phosphorylation sites in a protein.

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