|1za3, resolution 3.35Å ()|
The crystal structure of the YSd1 Fab bound to DR5
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 (K(D)=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.
Molecular recognition by a binary code., Fellouse FA, Li B, Compaan DM, Peden AA, Hymowitz SG, Sidhu SS, J Mol Biol. 2005 May 20;348(5):1153-62. Epub 2005 Apr 1. PMID:15854651
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
[TR10B_HUMAN] Receptor for the cytotoxic ligand TNFSF10/TRAIL. The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specific cysteine proteases) mediating apoptosis. Promotes the activation of NF-kappa-B. Essential for ER stress-induced apoptosis.
About this Structure
- Fellouse FA, Li B, Compaan DM, Peden AA, Hymowitz SG, Sidhu SS. Molecular recognition by a binary code. J Mol Biol. 2005 May 20;348(5):1153-62. Epub 2005 Apr 1. PMID:15854651 doi:10.1016/j.jmb.2005.03.041