Solution structure of human insulin-like growth factor 1: a nuclear magnetic resonance and restrained molecular dynamics study.
The solution structure of human insulin-like growth factor 1 has been investigated with a combination of nuclear magnetic resonance and restrained molecular dynamics methods. The results show that the solution structure is similar to that of insulin, but minor differences exist. The regions homologous to insulin are well-defined, while the remainder of the molecule exhibits greater disorder. The resultant structures have been used to visualize the sites for interaction with a number of physiologically important proteins.
Cooke
R M
RM
Department of Biochemistry, University of Oxford, U.K.
Harvey
T S
TS
Campbell
I D
ID
D000595:Amino Acid Sequence; D001665:Binding Sites; D006801:Humans; D007328:Insulin / Q000737:chemistry*; D007334:Insulin-Like Growth Factor I / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D011487:Protein Conformation; D012689:Sequence Homology, Nucleic Acid; D012996:Solutions; D013329:Structure-Activity Relationship
D007328:Insulin; D012996:Solutions; D007334:Insulin-Like Growth Factor I