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Detalle de: Structural context of exons in protein domains: Implications for protein modelling and design

Title Structural context of exons in protein domains: Implications for protein modelling and design
Abstract

Intron boundaries were extracted from genomic data and mapped onto single-domain human and murine protein structures taken from the Protein Data Bank. A first analysis of this set of proteins shows that intron boundaries prefer to be in non-regular secondary structure elements, while avoiding alpha-helices and beta-strands. This fact alone suggests an evolutionary model in which introns are constrained by protein structure, particularly by tertiary structure contacts. In addition, in silico recombination experiments of a subset of these proteins together with their homologues, including those in different species, show that introns have a tendency to occur away from artificial crossover hot spots. Altogether, these findings support a model in which genes can preferentially harbour introns in less constrained regions of the protein fold they code for. In the light of these findings, we discuss some implications for protein modelling and design.

Apa Reference Contreras-Moreira, B., Jonsson, P. F., & Bates, P. A. (2003). Structural Context of Exons in Protein Domains: Implications for Protein Modelling and Design. Journal of Molecular Biology, 333(5), 1045–1059. 10.1016/j.jmb.2003.09.023
Doi 10.1016/j.jmb.2003.09.023
Publication Date Nov 2003
Publication Type Article
Researcher Bruno Contreras Moreira
Ontology Genomics, Structural bioinformatics, Computational models and simulations, Evolutionary modelling
Research Groups Computational and structural biology @EEAD-CSIC
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