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| [[Image:1j1x.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1j1x| PDB=1j1x | SCENE= }} | | {{STRUCTURE_1j1x| PDB=1j1x | SCENE= }} |
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| '''Crystal Structure of HyHEL-10 Fv mutant LS93A complexed with hen egg white lysozyme'''
| | ===Crystal Structure of HyHEL-10 Fv mutant LS93A complexed with hen egg white lysozyme=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_12444085}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 12444085 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_12444085}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Yokota, A.]] | | [[Category: Yokota, A.]] |
| [[Category: Antigen-antibody complex]] | | [[Category: Antigen-antibody complex]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:42:18 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 14:22:41 2008'' |