The robustness and innovability of protein folds

作者：Toth Petroczy Agnes; Tawfik Dan S^*

来源：Current Opinion in Structural Biology, 2014, 26: 131-138.

DOI：10.1016/j.sbi.2014.06.007

Assignment of protein folds to functions indicates that >60% of folds carry out one or two enzymatic functions, while few folds, for example, the TIM-barrel and Rossmann folds, exhibit hundreds. Are there structural features that make a fold amenable to functional innovation (innovability)? Do these features relate to robustness - the ability to readily accumulate sequence changes? We discuss several hypotheses regarding the relationship between the architecture of a protein and its evolutionary potential. We describe how, in a seemingly paradoxical manner, opposite properties, such as high stability and rigidity versus conformational plasticity and structural order versus disorder, promote robustness and/or innovability. We hypothesize that polarity - differentiation and low connectivity between a protein's scaffold and its active-site - is a key prerequisite for innovability.

• 出版日期2014-6