Article
Phosphorylation-induced conformational dynamics in an intrinsically disordered protein and potential role in phenotypic heterogeneity.
Proceedings of the National Academy of Sciences of the United States of America - 28 Mar 2017
Kulkarni Prakash, Jolly Mohit Kumar, Jia Dongya, Mooney Steven M, Bhargava Ajay, Kagohara Luciane T, Chen Yihong, Hao Pengyu, He Yanan, Veltri Robert W, Grishaev Alexander, Weninger Keith, Levine Herbert, Orban John
Abstract excerpt
Intrinsically disordered proteins (IDPs) that lack a unique 3D structure and comprise a large fraction of the human proteome play important roles in numerous cellular functions. Prostate-Associated Gene 4 (PAGE4) is an IDP that acts as a potentiator of the Activator Protein-1 (AP-1) transcription factor. Homeodomain-Interacting Protein Kinase 1 (HIPK1) phosphorylates PAGE4 at S9 and T51, but only T51 is critical...
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