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Insulin has a concentration of 10-8-10-11 M in the blood which ensures that it circulates and exerts its physiological functions in vivo as a monomer. The crystal structure of monomeric porcine desB1-B2 despentapeptide (B26-B30) insulin (DesB1-2 DPI) with Mr = 4934 Da has been determined at 1.65 Å resolution using the molecular replacement method. A structural comparison between DesB1-2 DPI and 2Zn insulin reveals that the conformation of DesB1-2 DPI is more similar to molecule I than molecule II of 2Zn insulin. The remarkable conformational difference between B25-Phe in DesB1-2 DPI and B25-Phe in despentapeptide (B26-B30) insulin (DPI) indicates that the residue B25-Phe possesses great flexibility and mobility.

Supporting information

PDB reference: 1sbd

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