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

@article{Brinkman1991SitedirectedMO,
  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},
  year={1991},
  volume={291}
}
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37 Citations

Structure-Function Analysis of the Human Insulin-like Growth Factor Binding Protein-4*

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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.

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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*

TLDR
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)

TLDR
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.

Chapter 5 Molecular aspects of insulin-like growth factor binding proteins

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*

TLDR
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.

TLDR
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?

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    Growth hormone & IGF research : official journal of the Growth Hormone Research Society and the International IGF Research Society
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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.

TLDR
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.

Zinc alters the kinetics of IGF-II binding to cell surface receptors and binding proteins

TLDR
Findings imply that Zn2+ acts in vivo to prevent secreted IGF-II from binding to IGFBP-3 and IGF BP-5, thus maintaining IGF- II in an “active state,” i.e., readily available for IGF-1R association.

References

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TLDR
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.

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TLDR
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TLDR
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TLDR
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