1j1p
From Proteopedia
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'''Crystal structure of HyHEL-10 Fv mutant LS91A complexed with hen egg white lysozyme''' | '''Crystal structure of HyHEL-10 Fv mutant LS91A complexed with hen egg white lysozyme''' | ||
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[[Category: Tsumoto, K.]] | [[Category: Tsumoto, K.]] | ||
[[Category: Yokota, A.]] | [[Category: Yokota, A.]] | ||
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Revision as of 17:41, 2 May 2008
Crystal structure of HyHEL-10 Fv mutant LS91A complexed with hen egg white lysozyme
Overview
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.
About this Structure
1J1P is a Protein complex structure of sequences from Gallus gallus and Mus musculus. Full crystallographic information is available from OCA.
Reference
The role of hydrogen bonding via interfacial water molecules in antigen-antibody complexation. The HyHEL-10-HEL interaction., Yokota A, Tsumoto K, Shiroishi M, Kondo H, Kumagai I, J Biol Chem. 2003 Feb 14;278(7):5410-8. Epub 2002 Nov 19. PMID:12444085 Page seeded by OCA on Fri May 2 20:41:50 2008
