Structure and energetics of a non-proline cis-peptidyl linkage in a proline-202-->alanine carbonic anhydrase II variant.

@article{Tweedy1993StructureAE,
  title={Structure and energetics of a non-proline cis-peptidyl linkage in a proline-202-->alanine carbonic anhydrase II variant.},
  author={Neil Tweedy and Satheesh K Nair and S A Paterno and Carol A. Fierke and David W Christianson},
  journal={Biochemistry},
  year={1993},
  volume={32 41},
  pages={
          10944-9
        }
}
The crystal structure of a human carbonic anhydrase II (CAII) variant, cis-proline-202-->alanine (P202A), has been determined at 1.7-A resolution, indicating that the wild-type geometry, including the cis-peptidyl linkage, is retained upon substitution of proline by alanine. The CO2 hydrase activity and affinity for sulfonamide inhibitors of P202A CAII are virtually identical to those of wild type. However, the substitution of cis-alanine for cis-proline decreases the stability of the folded… CONTINUE READING