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

  title={Site‐directed mutagenesis of the N‐terminal region of IGF binding protein 1; analysis of IGF binding capability},
  author={Arend Brinkman and D J Kortleve and Alwin G. Schuller and Ellen C. Zwarthoff and Stenvert L. S. Drop},
  journal={FEBS Letters},
Localization of the IGF binding domain and evaluation of the role of cysteine residues in IGF binding in IGF binding protein-4.
This study sought to further localize the IGF binding domain and to evaluate the role of Cys residues in IGF binding, and speculate that the structural determinants of IGF-I and IGF-II binding in IGFBP-4 are very similar, if not identical.
Structure-Function Analysis of the Human Insulin-like Growth Factor Binding Protein-4*
The N-terminal sequence (Leu72–Ser91) and the C-terminale sequence (Cys205–Val214) are necessary to form the high affinity IGF binding domain, which is the major structural determinant of the IGFBP-4 function.
Ligand-binding characteristics of recombinant amino- and carboxyl-terminal fragments of human insulin-like growth factor-binding protein-3.
It is concluded that the carboxyl-terminal domain of IGFBP-3 contains an IGF-binding determinant and can form ternary complexes with ALS.
Localization of an Insulin-like Growth Factor (IGF) Binding Site of Bovine IGF Binding Protein-2 Using Disulfide Mapping and Deletion Mutation Analysis of the C-terminal Domain*
It is found that C-terminal truncation mutants designed and expressed in COS-1 mammalian cells lacked the IGF-II binding preference of WT bIGFBP-2, but appeared to play a role in determining IGF binding specificity as their removal resulted in mutants with higher IGF- II binding affinity.
Biochemical Studies on IGF and IGF-Binding Proteins Interactions & Structural Investigations on the SH3 Domain of Crk-associated Tyrosine Kinase Substrate p130cas (CAS)
A high resolution X-ray structure of the recombinant human CASSH3 domain has been determined providing a framework for the study of CAS SH3 domain protein-protein interactions, including applications of drug design.
BIAcore Analysis of Bovine Insulin-like Growth Factor (IGF)-binding Protein-2 Identifies Major IGF Binding Site Determinants in Both the Amino- and Carboxyl-terminal Domains*
In the absence of a complete tertiary structure to define the molecular basis of the high affinity binding interaction between insulin-like growth factors (IGFs) and IGF-binding proteins (IGFBPs), binding of IGFs by discrete amino- terminal domains and carboxyl-terminal domains of bovine IGFBP-2 is investigated.
Sequence comparison and predicted structure for the four exon-encoded regions of human insulin-like growth factor binding protein 4.
The IGFBP exon-encoded regions were aligned and secondary structure predictions for hIGFBP-4 were developed yielding predicted 3D co-ordinates for each such region of hIGMFCB-4, the most conserved among the IGFBPs.
What's new in the IGF-binding proteins?
  • S. Rosenzweig
  • Biology
    Growth hormone & IGF research : official journal of the Growth Hormone Research Society and the International IGF Research Society
  • 2004
Amino- and carboxyl-terminal fragments of insulin-like growth factor (IGF) binding protein-3 cooperate to bind IGFs with high affinity and inhibit IGF receptor interactions.
It is demonstrated that isolated amino- terminal and carboxyl-terminal domains of IGFBP-3 cooperate in the presence of IGFs to form high-affinity complexes that retain the ability to block IGF activity.


Cloning, sequence analysis and expression of a cDNA encoding a novel insulin‐like growth factor binding protein (IGFBP‐2).
The complete primary structure of a novel human IGF‐binding protein (IGFBP‐2) from a cloned cDNA is determined and it is suggested that they represent a family of structurally related human IGFBPs.
Molecular cloning of a new human insulin-like growth factor binding protein.
Molecular cloning of the cDNAs encoding a novel insulin-like growth factor-binding protein from rat and human.
The overall sequence homology among the four rat IGFBPs is very similar, suggesting that their individual genes diverged from a single ancestral gene at about the same evolutionary time point.
Cloning and expression of the growth hormone-dependent insulin-like growth factor-binding protein.
The deduced protein sequence of BP-53 has 33% amino acid identity including conservation of all 18 cysteine residues with the recently cloned BP-28, a smaller human IGF-binding protein identified in amniotic fluid and also secreted by the cell line HEP G2.
IGFBP-1, an insulin like growth factor binding protein, is a cell growth inhibitor.