Title of article :
Molecular Recognition by a Binary Code
Author/Authors :
Frederic A. Fellouse، نويسنده , , Bing Li، نويسنده , , Deanne M. Compaan، نويسنده , , Andrew A. Peden، نويسنده , , Sarah G. Hymowitz، نويسنده , , Sachdev S. Sidhu، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 2005
Abstract :
Functional antibodies were obtained from a library of antigen-binding sites generated by a binary code restricted to tyrosine and serine. An antibody raised against human vascular endothelial growth factor recognized the antigen with high affinity (KD=60 nM) and high specificity in cell-based assays. The crystal structure of another antigen binding fragment in complex with its antigen (human death receptor DR5) revealed the structural basis for this minimalist mode of molecular recognition. Natural antigen-binding sites are enriched for tyrosine and serine, and we show that these amino acid residues are intrinsically well suited for molecular recognition. Furthermore, these results demonstrate that molecular recognition can evolve from even the simplest chemical diversity.
Keywords :
phage display , protein engineering , combinatorial mutagenesis , antibody library , Vascular endothelial growth factor
Journal title :
Journal of Molecular Biology
Journal title :
Journal of Molecular Biology