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pubmed-article:19654879pubmed:abstractTextKinase-inducible domain (KID) as transcriptional activator can stimulate target gene expression in signal transduction by associating with KID interacting domain (KIX). NMR spectra suggest that apo-KID is an unstructured protein. After post-translational modification by phosphorylation, KID undergoes a transition from disordered to well folded protein upon binding to KIX. However, the mechanism of folding coupled to binding is poorly understood.lld:pubmed
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pubmed-article:19654879pubmed:articleTitleMolecular dynamics simulation of phosphorylated KID post-translational modification.lld:pubmed
pubmed-article:19654879pubmed:affiliationCollege of Life Sciences and Biotechnology, Shanghai Jiaotong University, Shanghai, China. haifengchen@sjtu.edu.cnlld:pubmed
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