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Protein-protein Interfaces

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 Interfaces

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Proteoglycans

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Using a GFP-tagged TMEM184A Construct for Confirmation of Heparin Receptor Identity

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Published on: February 17, 2017

Interactions between heparan sulfate and proteins-design and functional implications.

Ulf Lindahl¹, Jin-ping Li

¹Department of Medical Biochemistry and Microbiology, University of Uppsala, Uppsala, Sweden.

International Review of Cell and Molecular Biology

|July 9, 2009

Summary

Heparan sulfate (HS) proteoglycans are crucial for animal development and homeostasis. Their varied structures influence protein interactions, raising questions about the functional significance of HS biosynthesis regulation.

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Detection of Glycosaminoglycans by Polyacrylamide Gel Electrophoresis and Silver Staining

Detection of Glycosaminoglycans by Polyacrylamide Gel Electrophoresis and Silver Staining

Published on: February 25, 2021

Area of Science:

Biochemistry
Cell Biology
Glycoscience

Background:

Heparan sulfate (HS) proteoglycans are vital components of cell surfaces and extracellular matrices in animals.
HS proteoglycans play essential roles in development and homeostasis, and are implicated in various diseases.
The functions of HS chains are mediated by ionic interactions with proteins like growth factors and their receptors.

Purpose of the Study:

To investigate the specificity of heparan sulfate-protein interactions.
To understand the role of structural variability in HS biosynthesis and function.

Main Methods:

In vitro binding experiments using defined saccharides.
Cell signaling assays in cell culture.
Gene disruption of biosynthetic enzymes followed by phenotype analysis.

Main Results:

HS-protein interactions exhibit varying degrees of structural specificity.
Some protein ligands require precisely defined HS structures.
Other ligands bind to variable HS domains without dependence on specific saccharide sequences.

Conclusions:

The structural diversity of heparan sulfate influences its interactions with protein ligands.
The functional significance of regulatory mechanisms in HS biosynthesis remains an open question.