Structural highlights
Function
INS_PIG Insulin decreases blood glucose concentration. It increases cell permeability to monosaccharides, amino acids and fatty acids. It accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The crystal structure of NPH-insulin, pig insulin cocrystallized with zinc, m-cresol and protamine, has been solved by molecular replacement and refined using restrained least-squares refinement methods. The final crystallographic R factor for all reflections between 2 and 10 A is 19.4%. The insulin molecules are arranged as hexamers with two tetrahedrally coordinated Zn atoms in the central channel and one m-cresol bound to each monomer near His B5. One protamine binding site has been unequivocally identified near a dimer-dimer interface, although most of the polypeptide is crystallographically disordered. The conformation of the insulin moiety and the structural differences between the three unique monomers have been analysed. The zinc and m-cresol environments are described and the nature of the protamine binding site is outlined.
Structure of porcine insulin cocrystallized with clupeine Z.,Balschmidt P, Hansen FB, Dodson EJ, Dodson GG, Korber F Acta Crystallogr B. 1991 Dec 1;47 ( Pt 6):975-86. PMID:1772633[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Balschmidt P, Hansen FB, Dodson EJ, Dodson GG, Korber F. Structure of porcine insulin cocrystallized with clupeine Z. Acta Crystallogr B. 1991 Dec 1;47 ( Pt 6):975-86. PMID:1772633
