1XGL

HUMAN INSULIN DISULFIDE ISOMER, NMR, 10 STRUCTURES

Summary for 1XGL

• Entry DOI: 10.2210/pdb1xgl/pdb
• Descriptor: INSULIN (2 entities in total)
• Functional Keywords: hormone, glucose metabolism
• Biological source: Homo sapiens (human); More
• Cellular location: Secreted: P01308 P01308
• Total number of polymer chains: 2
• Total formula weight: 5817.65

Authors

Hua, Q.X.,Gozani, S.N.,Chance, R.E.,Hoffmann, J.A.,Frank, B.H.,Weiss, M.A. (deposition date: 1996-10-10, release date: 1997-04-01, Last modification date: 2024-10-30)

Primary citation

Hua, Q.X.,Gozani, S.N.,Chance, R.E.,Hoffmann, J.A.,Frank, B.H.,Weiss, M.A.
Structure of a protein in a kinetic trap.
Nat.Struct.Biol., 2:129-138, 1995

PubMed Abstract: We have determined the structure of a metastable disulphide isomer of human insulin. Although not observed for proinsulin folding or insulin-chain recombination, the isomer retains ordered secondary structure and a compact hydrophobic core. Comparison with native insulin reveals a global rearrangement in the orientation of A- and B-chains. One face of the protein's surface is nevertheless in common between native and non-native structures. This face contains receptor-binding determinants, rationalizing the partial biological activity of the isomer. Structures of native and non-native disulphide isomers also define alternative three-dimensional templates. Threading of insulin-like sequences provide an experimental realization of the inverse protein-folding problem.

PubMed: 7749917
DOI: 10.1038/nsb0295-129

Experimental method

SOLUTION NMR