1ZA3

The crystal structure of the YSd1 Fab bound to DR5

Summary for 1ZA3

• Entry DOI: 10.2210/pdb1za3/pdb
• Related: 1d0g
• Descriptor: Fab-YSd1 light chain, Fab-YSd1 heavy chain, Tumor necrosis factor receptor superfamily member 10B (3 entities in total)
• Functional Keywords: phage display, protein engineering, combinatorial mutagenesis, antibody library, death receptor-5, immune system-signaling protein complex, immune system/signaling protein
• Biological source: Homo sapiens (human); More
• Cellular location: Membrane; Single-pass type I membrane protein: O14763
• Total number of polymer chains: 6
• Total formula weight: 126742.72

Authors

Fellouse, F.A.,Li, B.,Compaan, D.M.,Peden, A.A.,Hymowitz, S.G.,Sidhu, S.S. (deposition date: 2005-04-05, release date: 2005-06-14, Last modification date: 2024-11-06)

Primary citation

Fellouse, F.A.,Li, B.,Compaan, D.M.,Peden, A.A.,Hymowitz, S.G.,Sidhu, S.S.
Molecular recognition by a binary code.
J.Mol.Biol., 348:1153-1162, 2005

PubMed 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 (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.

PubMed: 15854651
DOI: 10.1016/j.jmb.2005.03.041

Experimental method

X-RAY DIFFRACTION (3.35 Å)