The in silico interaction analysis of CARMIL1 protein-containing leucine-rich repeat (LRR) regions with interleukin-1 receptor-associated kinase 1 (IRAK1) protein and LLR peptide

Objectives: Capping protein Arp2/3 and myosin-I linker 1 (CARMIL1) encoded by the CARMIL, is a major, multidomain, membrane-linked regulating actin assembly; however, its function in inflammatory signaling not fully elucidated. The leucine-rich repeat (LRR) region of CARMIL1 has been associated with interleukin (IL)-1 receptor-associated kinase (IRAK) fibroblasts many methods including tandem mass tag spectrometry, immunoprecipitation, CRISPR-Cas9. This study, therefore, set out to assess interaction each IRAK1 novel LRR peptide. Methods: molecular docking techniques were employed compare binding modes affinities 3D structure peptides protein. model peptide was predicted through Robetta tool considering structures these proteins. Results: As an overall conclusion docking, observed contact residues 1-2 human CARMIL1, whereas interact 1, 2, 10 regions CARMIL1. Conclusions: Our computational results suggest that LRRs are involved formation protein-peptide interfaces structural conformation.