TABLE 2

Comparison of KZ52 cocrystal contacts to binding dataa

TABLE 2
  • a All 15 predicted contact residues (<3.9 Å) from the KZ52-GP cocrystal structure (23) are shown, as well as the type of bond identified from analysis of the crystal structure and the KZ52 immunoreactivity data (with ranges [the maximum minus minimum values]) derived in the current study. Residues identified as critical for binding are shaded in gray. All residues in the cocrystal structure are predicted to make hydrogen bonds and/or van der Waals interactions, as indicated; no salt bridges are formed in the cocrystal structure.

  • b Wild-type residue T42 (T42A in our mutation library) was mutated to V42 in the GP crystal structure to eliminate glycosylation at N40 (23).

  • c Contact of the indicated residues with KZ52 is only through alpha-carbon interactions on GP, so mutation to alanine is less likely to disrupt the MAb-GP interaction.