The importance of being tyrosine: lessons in molecular recognition from minimalist synthetic binding proteins.

ABSTRACT: Combinatorial libraries built with severely restricted chemical diversity have yielded highly functional synthetic binding proteins. Structural analyses of these minimalist binding sites have revealed the dominant role of large tyrosine residues for mediating molecular contacts and of small serine/glycine residues for providing space and flexibility. The concept of using limited residue types to construct optimized binding proteins mirrors findings in the field of small molecule drug development, where it has been proposed that most drugs are built from a limited set of side chains presented by diverse frameworks. The physicochemical properties of tyrosine make it the amino acid that is most effective for mediating molecular recognition, and protein engineers have taken advantage of these

SUBMITTER: Koide S 

PROVIDER: S-EPMC2829252 | biostudies-literature | 2009 May

REPOSITORIES: biostudies-literature