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Protein Kinase A isoform dynamics and disease.
Author(s) -
Aoto Phillip,
Baker Blaine,
Taylor Susan
Publication year - 2020
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.2020.34.s1.06840
Subject(s) - gene isoform , protein kinase a , mutation , protein kinase r , kinase , microbiology and biotechnology , biology , chemistry , cyclin dependent kinase 2 , genetics , gene
A number of disease mutations in the alpha and beta isoforms of Protein Kinase A have recently been identified. We model these mutations and investigate changes in conformational and protein/ligand interaction dynamics. Changes in partner protein and substrate interactions due to mutation is confirmed by fluorescence polarization binding and competition assays. Computational and biochemical approaches reveal a potential common mechanism among the mutations leading to kinase dysfunction.