1htv: Difference between revisions
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'''CRYSTAL STRUCTURE OF DESTRIPEPTIDE (B28-B30) INSULIN''' | '''CRYSTAL STRUCTURE OF DESTRIPEPTIDE (B28-B30) INSULIN''' | ||
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[[Category: Liang, D.]] | [[Category: Liang, D.]] | ||
[[Category: Ye, J.]] | [[Category: Ye, J.]] | ||
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[[Category: | [[Category: Helix]] | ||
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Revision as of 16:13, 2 May 2008
CRYSTAL STRUCTURE OF DESTRIPEPTIDE (B28-B30) INSULIN
Overview
Destripeptide (B28-B30) insulin (DTRI) is an insulin analogue that has much weaker association ability than native insulin but keeps most of its biological activity. It can be crystallized from a solution containing zinc ions at near-neutral pH. Its crystal structure has been determined by molecular replacement and refined at 1.9 A resolution. DTRI in the crystal exists as a loose hexamer compared with 2Zn insulin. The hexamer only contains one zinc ion that coordinates to the B10 His residues of three monomers. Although residues B28-B30 are located in the monomer-monomer interface within a dimer, the removal of them can simultaneously weaken both the interactions between monomers within the dimer and the interactions between dimers. Because the B-chain C-terminus of insulin is very flexible, we take the DTRI hexamer as a transition state in the native insulin dissociation process and suggest a possible dissociation process of the insulin hexamer based on the DTRI structure.
About this Structure
1HTV is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of destripeptide (B28-B30) insulin: implications for insulin dissociation., Ye J, Chang W, Liang D, Biochim Biophys Acta. 2001 May 5;1547(1):18-25. PMID:11343787 Page seeded by OCA on Fri May 2 19:13:33 2008
