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Intrinsically Disordered Protein Ensembles Shape Evolutionary Rates Revealing Conformational Patterns.

Abstract：

:Intrinsically disordered proteins (IDPs) lack stable tertiary structure under physiological conditions. The unique composition and complex dynamical behaviour of IDPs make them a challenge for structural biology and molecular evolution studies. Using NMR ensembles, we found that IDPs evolve under a strong site-specific evolutionary rate heterogeneity, mainly originated by different constraints derived from their inter-residue contacts. Evolutionary rate profiles correlate with the experimentally observed conformational diversity of the protein, allowing the description of different conformational patterns possibly related to their structure-function relationships. The correlation between evolutionary rates and contact information improves when structural information is taken not from any individual conformer or the whole ensemble, but from combining a limited number of conformers. Our results suggest that residue contacts in disordered regions constrain evolutionary rates to conserve the dynamic behaviour of the ensemble and that evolutionary rates can be used as a proxy for the conformational diversity of IDPs.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Palopoli N,Marchetti J,Monzon AM,Zea DJ,Tosatto SCE,Fornasari MS,Parisi G

doi

10.1016/j.jmb.2020.166751

subject

Has Abstract

pub_date

2021-02-05 00:00:00

pages

166751

issue

3

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(20)30676-8

journal_volume

433

pub_type

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