Abstract
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.
Keywords: Insulin, X-ray crystallography, conformational state, metal binding, Sr2+, Ni2+ and Cu2+ complexes, Hexagonal crystal system, Trigonal crystal system, SDS, sodium dodecyl sulfate, AN helix, Tensed conformation, Relaxed conformation, T3R3, REFMAC, Phe B-25Insulin, X-ray crystallography, conformational state, metal binding, Sr2+, Ni2+ and Cu2+ complexes, Hexagonal crystal system, Trigonal crystal system, SDS, sodium dodecyl sulfate, AN helix, Tensed conformation, Relaxed conformation, T3R3, REFMAC, Phe B-25
Protein & Peptide Letters
Title: Metal Induced Conformational Changes in Human Insulin: Crystal Structures of Sr2+, Ni2+ and Cu2+ Complexes of Human Insulin
Volume: 18 Issue: 5
Author(s): Nagampalli Raghavendra Sashi Krishna, Vasantha Pattabhi and S. S. Rajan
Affiliation:
Keywords: Insulin, X-ray crystallography, conformational state, metal binding, Sr2+, Ni2+ and Cu2+ complexes, Hexagonal crystal system, Trigonal crystal system, SDS, sodium dodecyl sulfate, AN helix, Tensed conformation, Relaxed conformation, T3R3, REFMAC, Phe B-25Insulin, X-ray crystallography, conformational state, metal binding, Sr2+, Ni2+ and Cu2+ complexes, Hexagonal crystal system, Trigonal crystal system, SDS, sodium dodecyl sulfate, AN helix, Tensed conformation, Relaxed conformation, T3R3, REFMAC, Phe B-25
Abstract: 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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Raghavendra Sashi Krishna Nagampalli, Pattabhi Vasantha and S. Rajan S., Metal Induced Conformational Changes in Human Insulin: Crystal Structures of Sr2+, Ni2+ and Cu2+ Complexes of Human Insulin, Protein & Peptide Letters 2011; 18 (5) . https://dx.doi.org/10.2174/092986611794927929
DOI https://dx.doi.org/10.2174/092986611794927929 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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