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Mitochondrial ATP synthase. Quaternary structure of the F1 moiety at 3.6 A determined by x-ray diffraction analysis.
Bianchet M, et al. J Biol Chem 1991. Among authors: Ysern X. PMID 1834656 Free article.
Here we present an x-ray map of this complex enzyme at 3.6 A, which provides a much more informative description of its quaternary structure. The overall dimensions of the F1 molecule are 120 A x 120 A x 74 A. The enzyme exhibits 3-fold symmetry relating the three copies of each of the two major subunits, alpha and beta. ...
Here we present an x-ray map of this complex enzyme at 3.6 A, which provides a much more informative description of its quaternary st …
Hydrogen bonding and solvent structure in an antigen-antibody interface. Crystal structures and thermodynamic characterization of three Fv mutants complexed with lysozyme
Fields BA, et al. Biochemistry 1996. Among authors: Ysern X. PMID 8952503
Thermodynamic parameters for antibody-antigen association have been measured using isothermal titration calorimetry, giving equilibrium binding constants Kb (M-1) of 2.6 x 10(7) (VLY50S), 7.0 x 10(7) (VHY32A), and 4.0 x 10(6) (VHY101F). For the WT complex, Kb is 2.7 x 10(8) M-1; thus, the affinities of the mutant Fv fragments for HEL are 10-, 4-, and 70-fold lower than that of the original antibody, respectively. ...
Thermodynamic parameters for antibody-antigen association have been measured using isothermal titration calorimetry, giving equilibrium bind …
Crystallization and preliminary X-ray diffraction study of an idiotope-anti-idiotope Fv-Fv complex.
Goldbaum FA, et al. J Mol Biol 1994. Among authors: Ysern X. PMID 8071997
A complex between the Fv fragment of an anti-hen eggwhite lysozyme antibody (D1.3) and the Fv fragment of an antibody specific for an idiotypic determinant of D1.3 has been crystallized in a form suitable for X-ray diffraction analysis. ...
A complex between the Fv fragment of an anti-hen eggwhite lysozyme antibody (D1.3) and the Fv fragment of an antibody specific for an idioty …
Molecular basis of antigen mimicry by an anti-idiotope
Fields BA, et al. Nature 1995. Among authors: Ysern X. PMID 7536303
It has been proposed that an anti-idiotypic antibody, anti-anti-X, may resemble the external antigen X and thus carry its 'internal image', but this idea is not unequivocally supported by the three-dimensional structures of anti-idiotopic antibodies, either because the structures of the external antigen or of the anti-idiotopic antibody were unknown, or because the anti-idiotopic antibodies showed no resemblance to the external antigens (reviewed in ref. 10). ...
It has been proposed that an anti-idiotypic antibody, anti-anti-X, may resemble the external antigen X and thus carry its 'int …
Protein motion and lock and key complementarity in antigen-antibody reactions
Braden BC, et al. Pharm Acta Helv 1995 - Review. Among authors: Ysern X. PMID 7651966
By contrast, in an idiotope--anti-idiotope (antibody-antibody) reaction, which is entropically driven, the binding equilibrium constant is only 1.5 x 10(5) M-1 at 20 degrees C. ...Complementarity with lysozyme is closer to a "lock and key" model and results in high affinity (2-4 x 10(8) M-1). That with the anti-idiotopic antibody involves conformational changes at its combining site and it results in a lower association constant (1.5 x 10(5) M-1). ...
By contrast, in an idiotope--anti-idiotope (antibody-antibody) reaction, which is entropically driven, the binding equilibrium constant is o …
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