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

FEBS Letters

Schuller, A.G.P.²  Drop, S.L.S.²  Kortleve, D.J.²  Brinkman, A.²  Zwarthoff, E.C.¹ 

[1] Department of Pathology, Erasmus University/Sophia Childrens Hospital, Rotterdam, The Netherlands;Department of Pediatrics, Subdivision of Pediatric Endocrinology, Erasmus University/Sophia Childrens Hospital, Rotterdam, The Netherlands

关键词: IGF binding protein;    N-terminus deletion mutant;    Site-directed mutagenesis;    Point mutation;    IGF binding site;    Disulphide bond;   

DOI  :  10.1016/0014-5793(91)81298-M

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown