Article
Pathogenic mutations of human phosphorylation sites affect protein-protein interactions.
Nature communications - 11 Apr 2024
Rrustemi Trendelina, Meyer Katrina, Roske Yvette, Uyar Bora, Akalin Altuna, Imami Koshi, Ishihama Yasushi, Daumke Oliver, Selbach Matthias
Abstract excerpt
Despite their lack of a defined 3D structure, intrinsically disordered regions (IDRs) of proteins play important biological roles. Many IDRs contain short linear motifs (SLiMs) that mediate protein-protein interactions (PPIs), which can be regulated by post-translational modifications like phosphorylation. 20% of pathogenic missense mutations are found in IDRs, and understanding how such mutations affect PPIs is...
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