Mol Biol Evol. 2011 Jan;28(1):59-62. doi: 10.1093/molbev/msq291. Epub 2010 Oct 29.
Protein structure is generally more conserved than sequence, but for regions that can adopt different structures in different environments, does this hold true? Understanding how structurally disordered regions evolve altered secondary structure element propensities as well as conformational flexibility among paralogs are fundamental questions for our understanding of protein structural evolution. We have investigated the evolutionary dynamics of structural disorder in protein families containing both orthologs and paralogs using phylogenetic tree reconstruction, protein structure disorder prediction, and secondary structure prediction in order to shed light upon these questions. Our results indicate that the extent and location of structurally disordered regions are not universally conserved. As structurally disordered regions often have high conformational flexibility, this is likely to have an effect on how protein structure evolves as spatially altered conformational flexibility can also change the secondary structure propensities for homologous regions in a protein family.
蛋白质结构通常比序列更保守，但对于那些在不同环境下可以采用不同结构的区域，这种情况是否成立？了解结构无序区域如何进化改变了二级结构元素倾向以及旁系同源物之间的构象灵活性，是我们理解蛋白质结构进化的基本问题。我们使用系统发育树重建、蛋白质结构无序预测和二级结构预测，研究了包含直系同源物和旁系同源物的蛋白质家族中结构无序的进化动态，以期回答这些问题。我们的结果表明，结构无序区域的程度和位置并不是普遍保守的。由于结构无序区域通常具有高度的构象灵活性，这可能会对蛋白质结构的进化产生影响，因为空间改变的构象灵活性也可以改变蛋白质家族中同源区域的二级结构倾向。
