AI Article Synopsis
- Many studies show that post-translational modifications (PTMs) like phosphorylation influence protein function, but there's no agreement on how much they alter protein structure.
- The research specifically focuses on phosphorylation of serine, threonine, and tyrosine and examines how these modifications affect various geometric parameters of proteins.
- It was found that phosphorylation leads to varying degrees of structural changes in proteins, particularly around the modification site, and this can switch proteins from inactive to active states.
Article Abstract
Modification of the protein after synthesis (PTM) often affects protein function as supported by numerous studies. However, there is no consensus about the degree of structural protein changes after modification. For phosphorylation of serine, threonine, and tyrosine, which is a common PTM in the biology of living organisms, we consider topical issues related to changes in the geometric parameters of a protein (Rg, RMSD, C displacement, SASA). The effect of phosphorylation on protein geometry was studied both for the whole protein and at the local level (i.e., in different neighborhoods of the modification site). Heterogeneity in the degree of protein structural changes after phosphorylation was revealed, which allowed for us to isolate a group of proteins having pronounced local structural changes in the neighborhoods of up to 15 amino acid residues from the modification site. This is a comparative study of protein structural changes in neighborhoods of 3-15 amino acid residues from the modified site. Amino acid phosphorylation in proteins with pronounced local changes caused switching from the inactive functional state to the active one.
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|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC10668964 | PMC |
| http://dx.doi.org/10.3390/biom13111564 | DOI Listing |
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