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      https://www.ias.ac.in/article/fulltext/jcsc/092/04-05/0473-0483

    • Keywords

       

      Insulin; despentapeptide insulin; crystal structure; monomer

    • Abstract

       

      Insulin modified by the removal of its 5 B chain C terminal residues is monomeric but remains substantially potent. The crystal structures of the beef and insulin (dpi) with two molecules in the asymmetric unit has been determined by x-ray analysis. The 3-dimensional structure ofdpi proves to be generally similar to that of native molecule in 2Zn insulin. More detailed comparison reveals that the slight differences in the two independent molecules of beefdpi are distributed uniformly throughout the structure in contrast to insulin in 2Zn insulin, where the structural changes are concentrated in specific regions.

      The loss of symmetry in thedpi crystal appears to be the inability of the A9 serine to pack effectively in the C2 cell. The efficient packing of the sheepdpi molecule whose crystal structure has also been determined and where A9 is glycine supports this conclusion.

    • Author Affiliations

       

      RU Chang Bi1 2 Zbigniew Dauter1 3 Eleanor Dodson1 Guy Dodson1 Federico Gordiano1 4 Rod Hubbard1 Colin Reynolds1

      1. Department of Chemistry, University of York, Heslington, York - YO1 5DD, England
      2. Via Mezzocannone 4, Universita di Napoli, Napoli - 80134, Italy
      3. Institute of Biophysics, Academia Sinica, Peking, China
      4. Department of Biochemistry, Technical University of Gdansk, Gdansk, Poland
    • Dates

       
  • Journal of Chemical Sciences | News

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