Site-directed mutagenesis of the N-terminal region of IGF binding protein 1; analysis of IGF binding capability

FEBS Lett. 1991 Oct 21;291(2):264-8. doi: 10.1016/0014-5793(91)81298-m.

Abstract

To define domains involved in IGF binding 60 N-terminal amino acid residues of IGFBP-1 were deleted. This deletion resulted in loss of IGF binding suggesting that the N-terminus may enclose an IGF binding domain. However, most point mutations introduced in this region did not affect IGF binding. In contrast to Cys-34, only substitution of Cys-38 for a tyrosine residue abolished IGF binding. With the determination that all 18 cysteine residues are involved in disulphide bond formation our data suggest that, although not all cysteines contribute to the same extent, the ligand binding site may be spatially organized.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Carrier Proteins / chemistry
  • Carrier Proteins / genetics*
  • Cell Line
  • Chlorocebus aethiops
  • Chromosome Deletion
  • Disulfides / chemistry
  • Insulin-Like Growth Factor Binding Proteins
  • Molecular Sequence Data
  • Mutagenesis, Site-Directed*
  • Plasmids
  • Protein Binding

Substances

  • Carrier Proteins
  • Disulfides
  • Insulin-Like Growth Factor Binding Proteins