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- W2024051616 abstract "Membrane proteins evolved to function in a diverse phospholipid environment. Experimental evidence suggests that some phospholipid molecules are recruited by membrane proteins as co-factors or ligands that tightly bind to specific sites on the protein surface and play important functional roles. In this work we have assessed the evolutionary conservation of phospholipid-binding sites in several alpha-helical and beta-barrel membrane proteins. We first identified the membrane protein surface residues and residues that are in close contact with co-crystallized phospholipids in the x-ray structures of adrenergic receptor, photosynthetic reaction center, Kcsa potassium channel, formate dehydrogenase and ferric hydroxamate uptake receptor using methods of computational geometry such as Delaunay triangulation and alpha shape. We next collected orthologous cDNA sequences for every protein and used posterior probability analysis of evolutionary selection pressure measured as ω-ratio with the aid of PAML package to identify phospholipid-facing residues under strong purifying selection pressure. We show that protein residues interacting with co-crystallized phospholipids are collectively more conserved than the rest of the phospholipid-facing residues with statistically significant p-values in the range 10e-7 - 10e-3. Additionally, we found that every phospolipid-binding site on the membrane protein surface contains from 3 to 5 residues that experience strong purifying selection pressure similar to the functionally important buried residues." @default.
- W2024051616 created "2016-06-24" @default.
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- W2024051616 date "2010-01-01" @default.
- W2024051616 modified "2023-09-26" @default.
- W2024051616 title "Evolutionary Conservation of Phospholipid-Binding Sites in Membrane Proteins" @default.
- W2024051616 doi "https://doi.org/10.1016/j.bpj.2009.12.284" @default.
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