Elucidation of IGHV3-33 antibody binding modes to the NANP polypeptide. Crystal co-structure of MA6 bound to NPNA3 peptide. (A) Overview of peptide in groove. The peptide lies within a groove formed primarily by the heavy chain, with CDR-H3 residues forming one side of the groove and CDR-H1 and -H2 residues forming the other side. (B) Specific contacts. Compared to related structures, the MA6 Trp52 sidechain is flipped such that the pyrrole ring of the indole, rather than the benzene ring, packs against Pro6 of the peptide. (C) Superposition with 1210 Fab. MA6 and 1210 bind the peptide in an almost identical conformation (RMSD of 0.23 Å for the first 8 Cα atoms).
Figure 5.

Elucidation of IGHV3-33 antibody binding modes to the NANP polypeptide. Crystal co-structure of MA6 bound to NPNA3 peptide. (A) Overview of peptide in groove. The peptide lies within a groove formed primarily by the heavy chain, with CDR-H3 residues forming one side of the groove and CDR-H1 and -H2 residues forming the other side. (B) Specific contacts. Compared to related structures, the MA6 Trp52 sidechain is flipped such that the pyrrole ring of the indole, rather than the benzene ring, packs against Pro6 of the peptide. (C) Superposition with 1210 Fab. MA6 and 1210 bind the peptide in an almost identical conformation (RMSD of 0.23 Å for the first 8 Cα atoms).

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