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Related Concept Videos

Insulin: The Receptor and Signaling Pathways01:28

Insulin: The Receptor and Signaling Pathways

Insulin action is mediated through a receptor tyrosine kinase, akin to the IGF-1 receptor. The number of receptors per cell varies significantly, from 40 on erythrocytes to 300,000 on adipocytes and hepatocytes. The insulin receptor consists of linked α/β subunit dimers, forming a heterotetramer glycoprotein with two extracellular α subunits and two β subunits spanning the membrane. The α subunits inhibit the inherent tyrosine kinase activity of the β subunits, but this inhibition is released...
Protein and Protein Structure02:15

Protein and Protein Structure

Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme can...
Protein-protein Interfaces02:04

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
Protein-Protein Interfaces02:04

Protein-Protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
Ligand Binding Sites02:40

Ligand Binding Sites

Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
Ligand Binding Sites02:40

Ligand Binding Sites

Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...

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Updated: May 21, 2026

Precise Visualization of Insulin Receptors A and B in Murine Brain with an RNA In Situ Hybridization Assay
08:34

Precise Visualization of Insulin Receptors A and B in Murine Brain with an RNA In Situ Hybridization Assay

Published on: July 15, 2025

Insulin-like growth factor binding proteins: a structural perspective.

Briony E Forbes1, Peter McCarthy, Raymond S Norton

  • 1The School of Molecular and Biomedical Science, The University of Adelaide Adelaide, SA, Australia.

Frontiers in Endocrinology
|June 2, 2012
PubMed
Summary
This summary is machine-generated.

Insulin-like growth factor binding proteins (IGFBPs) regulate growth factor action. Structural studies reveal how IGFBPs bind insulin-like growth factors (IGFs) and other molecules, impacting cell growth and disease.

Keywords:
IGF binding proteininsulin-like growth factorprotein structure

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FIBS-enabled Noninvasive Metabolic Profiling
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Last Updated: May 21, 2026

Precise Visualization of Insulin Receptors A and B in Murine Brain with an RNA In Situ Hybridization Assay
08:34

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09:16

FIBS-enabled Noninvasive Metabolic Profiling

Published on: February 3, 2014

Area of Science:

  • Biochemistry and Molecular Biology
  • Structural Biology

Background:

  • Insulin-like growth factor binding proteins (IGFBP-1 to -6) are crucial regulators of insulin-like growth factors (IGF-I and IGF-II).
  • IGFBPs modulate IGF bioavailability, directing them to target tissues and influencing cell growth, proliferation, differentiation, and survival through the type 1 IGF receptor.
  • Beyond IGFs, IGFBPs exhibit IGF-independent activities, affecting cell migration and apoptosis by modulating gene transcription.

Purpose of the Study:

  • To review recent structural studies of IGFBPs.
  • To highlight structural features critical for IGF binding and interactions with other molecules.
  • To outline future directions for structural research on the IGFBP family.

Main Methods:

  • Analysis of solved crystal structures of individual IGFBP domains (N-terminal and C-terminal).
  • Examination of the solved structure of an IGFBP-N-BP-4:IGF-I:C-BP-4 complex.
  • Identification of structural features involved in binding IGFs, extracellular matrix components, and integrins.

Main Results:

  • While intact IGFBP structures remain elusive, structures of individual domains and a partial complex have provided detailed insights into the IGF binding site and mechanism.
  • Structural studies have identified key features enabling IGFBPs to interact with extracellular matrix proteins and integrins.
  • These structural findings elucidate both IGF-dependent and IGF-independent functions of IGFBPs.

Conclusions:

  • Structural biology has significantly advanced our understanding of IGFBP function over the last 15 years.
  • Knowledge of IGFBP structures is vital for comprehending their roles in normal growth, development, and various diseases.
  • Future structural studies promise to further elucidate the complex roles of the IGFBP family.