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- Title
Comparative Analysis and Molecular Evolution of Class I PI3K Regulatory Subunit p85α Reveal the Structural Similarity Between nSH2 and cSH2 Domains.
- Authors
Chakraborty, Chiranjib; Sharma, Ashish Ranjan; Sharma, Garima; Lee, Sang-Soo
- Abstract
Phosphoinositide 3-kinase (PI3K) is an essential regulatory protein of the insulin signaling pathway and several other pathways that govern cell survival, cell proliferation, cell differentiation and oncogene regulation. The protein has main two subunits; regulatory p85 and catalytic p110. Other regulatory subunits are p50, p55. The catalytic activity of p110 is stabilized by the regulatory subunit p85α. This regulatory subunit is composed of five domains; the SH3, BCR-homology (BH), N-terminal SH2 (nSH2), C-terminal SH2 (cSH2), and inter-SH2 (iSH2). In the current study, we executed comparative analysis of the computational proteomic and molecular evolution of these five domains. Our results reveal that faster and more cost-effective methods for forming intricate relationships between the domains are worth pursuing according to vital proteomic parameters such as physico-chemical properties, evolution and post-translational modification (PTM). The results show variation instability, grand average of hydrophobicity (GRAVY), aliphatic index, globularity, PTM among the five domains, and strongly indicate a likeness between the nSH2 and cSH2 domains. The study provides vital information for the structural and functional aspects of PI3K regulatory subunit p85α. Many of these property changes might be defined as protein–protein interactions, protein folding structures and structure–function correlations in future.
- Subjects
MOLECULAR evolution; PHOSPHATIDYLINOSITOL 3-kinases; INSULIN; POST-translational modification; PROTEIN structure; PROTEIN folding
- Publication
International Journal of Peptide Research & Therapeutics, 2020, Vol 26, Issue 4, p2555
- ISSN
1573-3149
- Publication type
Article
- DOI
10.1007/s10989-020-10039-1