2DQH

Crystal structure of hyhel-10 FV mutant (Hy58a) complexed with hen egg lysozyme

Summary for 2DQH

• Entry DOI: 10.2210/pdb2dqh/pdb
• Related: 1C08 2DQC 2DQD 2DQE 2DQF 2DQG 2DQI 2DQJ
• Descriptor: lysozyme binding Ig kappa chain V23-J2 region, Ig VH,anti-lysozyme, Lysozyme C, ... (4 entities in total)
• Functional Keywords: antigen-antibody complex, mutant, immune system-hydrolase complex, immune system/hydrolase
• Biological source: Mus musculus (house mouse); More
• Cellular location: Secreted: P00698
• Total number of polymer chains: 3
• Total formula weight: 38658.81

Authors

Shiroishi, M.,Kondo, H.,Tsumoto, K.,Kumagai, I. (deposition date: 2006-05-26, release date: 2007-01-23, Last modification date: 2024-10-23)

Primary citation

Shiroishi, M.,Tsumoto, K.,Tanaka, Y.,Yokota, A.,Nakanishi, T.,Kondo, H.,Kumagai, I.
Structural consequences of mutations in interfacial Tyr residues of a protein antigen-antibody complex. The case of HyHEL-10-HEL
J.Biol.Chem., 282:6783-6791, 2007

PubMed Abstract: Tyrosine is an important amino acid in protein-protein interaction hot spots. In particular, many Tyr residues are located in the antigen-binding sites of antibodies and endow high affinity and high specificity to these antibodies. To investigate the role of interfacial Tyr residues in protein-protein interactions, we performed crystallographic studies and thermodynamic analyses of the interaction between hen egg lysozyme (HEL) and the anti-HEL antibody HyHEL-10 Fv fragment. HyHEL-10 has six Tyr residues in its antigen-binding site, which were systematically mutated to Phe and Ala using site-directed mutagenesis. The crystal structures revealed several critical roles for these Tyr residues in the interaction between HEL and HyHEL-10 as follows: 1) the aromatic ring of Tyr-50 in the light chain (LTyr-50) was important for the correct ternary structure of variable regions of the immunoglobulin light chain and heavy chain and of HEL; 2) deletion of the hydroxyl group of Tyr-50 in the heavy chain (HTyr-50) resulted in structural changes in the antigen-antibody interface; and 3) the side chains of HTyr-33 and HTyr-53 may help induce fitting of the antibody to the antigen. Hot spot Tyr residues may contribute to the high affinity and high specificity of the antigen-antibody interaction through a diverse set of structural and thermodynamic interactions.

PubMed: 17166830
DOI: 10.1074/jbc.M605197200

Experimental method

X-RAY DIFFRACTION (2.3 Å)