Conformational correlation and coupled motion between residue A21 and B25 side chain observed in crystal structures of insulin mutants at position A21.

@article{Zeng2000ConformationalCA,
  title={Conformational correlation and coupled motion between residue A21 and B25 side chain observed in crystal structures of insulin mutants at position A21.},
  author={Z H Zeng and Yuan Shuai Liu and Liqin Jin and Y Zhang and Svend Havelund and J. B. Markussen and Da Cheng Wang},
  journal={Biochimica et biophysica acta},
  year={2000},
  volume={1479 1-2},
  pages={225-36}
}
The C-terminal residue of the insulin A chain is invariant and kept as asparagine in all known insulin molecules from hagfish through birds to mammals. To get information on the role of this conserved residue, which is still unclear, the three-dimensional structures of four human insulin mutants, A21 Asn-->Gly, A21 Asn-->Asp, A21 Asn-->Ala, and A21 Asn… CONTINUE READING