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- W2292512574 abstract "We addressed the evolutionary trace of hetero-oligomer interfaces by comparing the structures of paralogous proteins; one of them is a monomer or homo-oligomer and the other is a hetero-oligomer. We found different trends in amino acid conservation pattern and hydrophobicity between homo-oligomer and hetero-oligomer. The degree of amino acid conservation in the interface of homo-oligomer has no obvious difference from that in the surface, whereas the degree of conservation is much higher in the interface of hetero-oligomer. The interface of homo-oligomer has a few very conserved residue positions, whereas the residue conservation in the interface of hetero-oligomer tends to be higher. In addition, the interface of hetero-oligomer has a tendency of being more hydrophobic compared with the one in homo-oligomer. We conjecture that these differences are related to the inherent symmetry in homo-oligomers that cannot exist in hetero-oligomers. Paucity of the structural data precludes statistical tests of these tendencies, yet the trend can be applied to the prediction of the interface of hetero-oligomer. We obtained putative interfaces of the subunits in CPSF (cleavage and polyadenylation specificity factor), one of the human pre-mRNA 3'-processing complexes. The locations of predicted interface residues were consistent with the known experimental data." @default.
- W2292512574 created "2016-06-24" @default.
- W2292512574 creator A5027798404 @default.
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- W2292512574 date "2015-01-01" @default.
- W2292512574 modified "2023-09-26" @default.
- W2292512574 title "Case study on the evolution of hetero-oligomer interfaces based on the differences in paralogous proteins" @default.
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- W2292512574 doi "https://doi.org/10.2142/biophysico.12.0_103" @default.
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