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PDBsum entry 1vfb
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Immunoglobulin/hydrolase(o-glycosyl)
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PDB id
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1vfb
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Contents |
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107 a.a.
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116 a.a.
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129 a.a.
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Bound water molecules and conformational stabilization help mediate an antigen-Antibody association.
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Authors
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T.N.Bhat,
G.A.Bentley,
G.Boulot,
M.I.Greene,
D.Tello,
W.Dall'Acqua,
H.Souchon,
F.P.Schwarz,
R.A.Mariuzza,
R.J.Poljak.
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Ref.
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Proc Natl Acad Sci U S A, 1994,
91,
1089-1093.
[DOI no: ]
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PubMed id
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Abstract
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We report the three-dimensional structures, at 1.8-A resolution, of the Fv
fragment of the anti-hen egg white lysozyme antibody D1.3 in its free and
antigen-bound forms. These structures reveal a role for solvent molecules in
stabilizing the complex and provide a molecular basis for understanding the
thermodynamic forces which drive the association reaction. Four water molecules
are buried and others form a hydrogen-bonded network around the interface,
bridging antigen and antibody. Comparison of the structures of free and bound Fv
fragment of D1.3 reveals that several of the ordered water molecules in the free
antibody combining site are retained and that additional water molecules link
antigen and antibody upon complex formation. This solvation of the complex
should weaken the hydrophobic effect, and the resulting large number of
solvent-mediated hydrogen bonds, in conjunction with direct protein-protein
interactions, should generate a significant enthalpic component. Furthermore, a
stabilization of the relative mobilities of the antibody heavy- and light-chain
variable domains and of that of the third complementarity-determining loop of
the heavy chain seen in the complex should generate a negative entropic
contribution opposing the enthalpic and the hydrophobic (solvent entropy)
effects. This structural analysis is consistent with measurements of enthalpy
and entropy changes by titration calorimetry, which show that enthalpy drives
the antigen-antibody reaction. Thus, the main forces stabilizing the complex
arise from antigen-antibody hydrogen bonding, van der Waals interactions,
enthalpy of hydration, and conformational stabilization rather than solvent
entropy (hydrophobic) effects.
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Secondary reference #1
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Title
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Small rearrangements in structures of fv and FAB fragments of antibody d1.3 on antigen binding.
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Authors
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T.N.Bhat,
G.A.Bentley,
T.O.Fischmann,
G.Boulot,
R.J.Poljak.
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Ref.
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Nature, 1990,
347,
483-485.
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PubMed id
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