The three-dimensional structure of a complex of a murine Fab (NC10.14) with a potent sweetener (NC174): an illustration of structural diversity in antigen recognition by immunoglobulins

Three‐dimensional structures of carbohydrate determinants of Lewis system antigens: Implications for effective antibody targeting of cancer

“…Such diverse recognition strategies are generally accepted to form the repertoire of antibodies raised against the same or structurally similar antigens. 52 However, as observed with hu3S193 and BR96, it is also possible for remarkable structural convergence to occur in antibodies elicited against Le y -positive tumour cells. 46 Comparisons of the hu3S193 and BR96 45 antibodies bound to Le y ligands revealed extremely similar mechanisms for recognition of the carbohydrate determinant.…”

Capsid Antibodies to Different Adeno-Associated Virus Serotypes Bind Common Regions

“…Positive difference density, representing portions of structure not accounted for by the capsid atomic model, was interpreted as the bound Fab. Initial pseudoatomic modeling of the Fab densities used the coordinates of three generic Fab structures (PDB 2FBJ (IgA) (77), 8FAB (IgG1) (78), and 1ETZ (IgG2B) (79) to assess different elbow angles and variable region structures and, in particular, the complementarity-determining region 3 (CDR3). For AAV2:C37B (for which there was no WAM model), density corresponding to a single Fab was extracted from the reconstruction using the voledit program in SITUS (74), and the 2FBJ Fab coordinates were manually fit within the density, followed by refinement with the "fit-in-map" function in Chimera (80).…”

Incorporation of Long CDR3s into V Domains: Implications for the Structural Evolution of the Antibody-Combining Site

“…We speculate that these disulfide linkages emerged in order to rigidify the combining site or at least help stabilize extremely long HCDR3 segments. We have recently observed that a 16-residue HCDR3 of a murine monoclonal Fab (NC10.14) was an almost perfect mimic for the last ß-hairpin turn in the C domain of its own Ï light chain, which is a region that is structurally homologous to the loop containing HCDR3 [28]. These observations support the ideas that primordial V and C domains were truly more similar than they are in contemporary antibodies and that HCDR3s were longer and even more dominant features.…”

“…We have recently described the structural convergence of an HCDR3 in a murine VH domain and the final ß-hairpin of the CÏ domain of a single antibody molecule (PDB code 1ETZ [28]). Namely, in the crystal structure of the NC10.14 Fab complexed with a superpotent sweetener compound (NC174), the 16-residue HCDR3 is composed of two antiparallel ß-strands connected by a type 1) ß-turn at the apex.…”