1j1x: Difference between revisions

Revision as of 14:18, 21 February 2008

Crystal Structure of HyHEL-10 Fv mutant LS93A complexed with hen egg white lysozyme

OverviewOverview

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 StructureAbout this Structure

1J1X is a Protein complex structure of sequences from Gallus gallus and Mus musculus. Active as Lysozyme, with EC number 3.2.1.17 Full crystallographic information is available from OCA.

ReferenceReference

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

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 '''Crystal Structure of HyHEL-10 Fv mutant LS93A complexed with hen egg white lysozyme'''<br />
 ==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.
+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==
-J1X is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Active as [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1J1X OCA].
+J1X is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Active as [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J1X OCA].
 ==Reference==
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 [[Category: antigen-antibody complex]]
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