1J1P
Crystal structure of HyHEL-10 Fv mutant LS91A complexed with hen egg white lysozyme
Summary for 1J1P
| Entry DOI | 10.2210/pdb1j1p/pdb |
| Related | 1C08 1J1O 1J1X |
| Descriptor | lysozyme binding Ig kappa chain V23-J2 region, Ig VH,anti-lysozyme, Lysozyme C, ... (4 entities in total) |
| Functional Keywords | antigen-antibody complex, 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 | 38734.91 |
| Authors | Yokota, A.,Tsumoto, K.,Shiroishi, M.,Kondo, H.,Kumagai, I. (deposition date: 2002-12-13, release date: 2003-01-14, Last modification date: 2023-12-27) |
| Primary citation | Yokota, A.,Tsumoto, K.,Shiroishi, M.,Kondo, H.,Kumagai, I. The Role of Hydrogen Bonding via Interfacial Water Molecules in Antigen-Antibody Complexation. THE HyHEL-10-HEL INTERACTION J.BIOL.CHEM., 278:5410-5418, 2003 Cited by PubMed Abstract: To study the role of hydrogen bonding via interfacial water molecules in protein-protein interactions, we examined the interaction between hen egg white lysozyme (HEL) and its HyHEL-10 variable domain fragment (Fv) antibody. We constructed three antibody mutants (l-Y50F, l-S91A, and l-S93A) and investigated the interactions between the mutant Fvs and HEL. Isothermal titration calorimetry indicated that the mutations significantly decreased the negative enthalpy change (8-25 kJ mol(-1)), despite some offset by a favorable entropy change. X-ray crystallography demonstrated that the complexes had nearly identical structures, including the positions of the interfacial water molecules. Taken together, the isothermal titration calorimetric and x-ray crystallographic results indicate that hydrogen bonding via interfacial water enthalpically contributes to the Fv-HEL interaction despite the partial offset because of entropy loss, suggesting that hydrogen bonding stiffens the antigen-antibody complex. PubMed: 12444085DOI: 10.1074/jbc.M210182200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
Download full validation report
