By Frank J. Dixon (Eds.)
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Additional info for Advances in Immunology
1987). , 1972). The MHr protein fold consists of an antiparallel bundle of four a-helices (named A, B, C, and D in sequence order) that surround a two-iron center a t the active site, an N-terminal loop region, and shorter loops between the helices and a t the Cterminus. , 1987a). , 1985). , 1985a). Examination of the exposed MHr molecular surface and corrected average main-chain temperature factors by residue indicates that a large portion (over 80%) of the molecular surface is relatively mobile.
Getzoff, A. Feinstein, and J. 7. Crystal packing for the Fab Kol. , 1980), the antigen combining site shows direct interactions with neighboring molecules in the crystal. In this cross-section of the crystal lattice, the a-carbon backbones are color coded to show the location of the framework and CDR residues for the light chains (lavender framework bonds and green CDRs) and the heavy chains (light blue framework bonds and red CDRs). Crystal packing places the CDRs from o n e 9 a b against the C, and C,,1 of the next.
3 antibody, and replacement of a lysozyme arginine residue by a lysine similarly affected binding by the HyHEL5 antibody. Thus, to understand the interaction chemistry, it is necessary to define the amino acids critical to the binding energy (the antigenic determinants in a chemical sense) and not simply to identify the residues buried in the interface. , that not all interacting residues are contributing fully to the binding affinity. One technical point should be appreciated: a protein interface does not have a unique quantitative definition.
Advances in Immunology by Frank J. Dixon (Eds.)