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Metal Induced Conformational Changes in Human Insulin: Crystal Structures of Sr2+, Ni2+ and Cu2+ Complexes of Human Insulin

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Crystal structures of Sr2+, Ni2+ and Cu2+ of human insulin complexes have been determined. The structures of Sr2+ and Ni2+ complexes are similar to Zn2+ insulin and are in T6 conformation. (All the six monomers in the insulin hexamer are in Tensed conformation (T), which means the first eight residues of B-chain are in an extended conformation). Cu2+ complex, though it assumes T6 conformation, has more structural differences due to lowering of crystal symmetry and space group shift from H3 (Hexagonal crystal system) to P3 (Trigonal crystal system) and a doubling of the c axis. 2Ni2+ human insulin when compared to 4Ni2+ Arg insulin suggests that terminal modifications may be responsible for additional metal binding. All the three metals have been shown to have a role in diabetes and hence may be therapeutically useful.

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Keywords: AN helix; Hexagonal crystal system; Insulin; Phe B-25; REFMAC; Relaxed conformation; SDS; Sr2+; Ni2+ and Cu2+ complexes; T3R3; Tensed conformation; Trigonal crystal system; X-ray crystallography; conformational state; metal binding; sodium dodecyl sulfate

Document Type: Research Article

Publication date: 2011-05-01

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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