Conformational diversity and the emergence of sequence signatures during evolution. (June 2015)

• Record Type: Journal Article
• Authors: Parisi, Gustavo; Zea, Diego Javier; Monzon, Alexander Miguel; Marino-Buslje, Cristina
• Is Part Of: Current opinion in structural biology. Volume 32(2015)
• Page Start: 58
• Page End: 65
• Publication Date: 2015-06
• Subjects: Molecular biology -- Periodicals; 570
• DOI: 10.1016/j.sbi.2015.02.005
• Languages: English
• ISSNs: 0959-440X

Abstract

Highlights: Protein's native structure is an ensemble of conformers with similar energies. Conformational diversity constraints sequence divergence. High conformational diversity correlates with slow evolution. Residues coevolution networks form spatial clusters in the protein structure. Coevolutionary analysis captures residue–residue correlations within different conformations. Abstract : Proteins' native structure is an ensemble of conformers in equilibrium, including all their respective functional states and intermediates. The induced-fit first and the pre-equilibrium theories later, described how structural changes are required to explain the allosteric and cooperative behaviours in proteins, which are key to protein function. The conformational ensemble concept has become a key tool in explaining an endless list of essential protein properties such as function, enzyme and antibody promiscuity, signal transduction, protein–protein recognition, origin of diseases, origin of new protein functions, evolutionary rate and order–disorder transitions, among others. Conformational diversity is encoded by the amino acid sequence and such a signature can be evidenced through evolutionary studies as evolutionary rate, conservation and coevolution.