6INS

X-RAY ANALYSIS OF THE SINGLE CHAIN B29-A1 PEPTIDE-LINKED INSULIN MOLECULE. A COMPLETELY INACTIVE ANALOGUE

Summary for 6INS

• Entry DOI: 10.2210/pdb6ins/pdb
• Descriptor: INSULIN, ZINC ION (3 entities in total)
• Functional Keywords: hormone
• Biological source: Sus scrofa (pig)
• Cellular location: Secreted: P01315
• Total number of polymer chains: 2
• Total formula weight: 11527.88

Authors

Derewenda, U.,Derewenda, Z.,Dodson, E.J.,Dodson, G.G.,Bing, X.,Markussen, J. (deposition date: 1992-11-25, release date: 1994-01-31, Last modification date: 2024-10-16)

Primary citation

Derewenda, U.,Derewenda, Z.,Dodson, E.J.,Dodson, G.G.,Bing, X.,Markussen, J.
X-ray analysis of the single chain B29-A1 peptide-linked insulin molecule. A completely inactive analogue.
J.Mol.Biol., 220:425-433, 1991

PubMed Abstract: A crystal structure of a totally inactive insulin molecule has been determined. For this insulin molecule, the first without detectable activity to be characterized, the A and B-chains are linked by a peptide bond between A1 Gly and B29 Lys. The molecule has retained all its normal self-association properties and it can also accommodate the two different conformations designated T and R, as seen in 4Zn native pig insulin crystals. The hexamers of the crosslinked insulin molecule were crystallized using the 4Zn insulin recipe of Schlichtkrull. The structure has been crystallographically refined with data extending to 2 A using restrained least-square methods. Comparison of the B29-A1 peptide crosslink insulin and the 4Zn native insulin reveals close structural similarities with the native dimer. The analysis of the structure confirms the earlier hypothesis that insulin structures in crystals are not in an active conformation and that a separation of N-terminal A-chain and C-terminal B-chain is required for interaction with the insulin receptor.

PubMed: 1856866
DOI: 10.1016/0022-2836(91)90022-X

Experimental method

X-RAY DIFFRACTION (2 Å)