1HTV

CRYSTAL STRUCTURE OF DESTRIPEPTIDE (B28-B30) INSULIN

Summary for 1HTV

• Entry DOI: 10.2210/pdb1htv/pdb
• Descriptor: INSULIN, ZINC ION, ... (4 entities in total)
• Functional Keywords: helix, beta sheet, hormone-growth factor complex, hormone/growth factor
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 12
• Total formula weight: 33006.92

Authors

Ye, J.,Chang, W.,Liang, D. (deposition date: 2001-01-01, release date: 2001-05-23, Last modification date: 2024-04-03)

Primary citation

Ye, J.,Chang, W.,Liang, D.
Crystal structure of destripeptide (B28-B30) insulin: implications for insulin dissociation.
Biochim.Biophys.Acta, 1547:18-25, 2001

PubMed Abstract: 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.

PubMed: 11343787
DOI: 10.1016/S0167-4838(01)00160-1

Experimental method

X-RAY DIFFRACTION (1.9 Å)