Universally expressed by all mammalian cells, heparan sulfate (HS) is a major and often dominant component of the landscape at the cell surface and thus plays essential roles in cell signaling and cell-cell interactions. At the cell surface and in the extracellular matrix, HS exerts its biological functions by interacting with hundreds of HS-binding proteins, which include growth factors, chemokines, cytokines, coagulation factors, complements, enzymes, enzyme inhibitors, transmembrane receptors, decoy receptors, adhesion molecules, and matrix proteins. One unique feature of HS-binding proteins is they are structurally highly diverse because HS-binding capability can arise from almost any protein fold. Understanding the structural basis of HS-protein interaction is often the key to elucidating the physiological significance of a particular HS-protein interaction.
It is apparent that without a sophisticated understanding of the structural basis of particular HS-protein interactions, it is difficult to gain any significant insight on how HS regulates the pathophysiological roles of the HS-binding protein in question. Such insight is also critical if one desires to alter the biological functions of HS-binding proteins by manipulating HS-protein interactions. In the past decade, many new biophysical and biochemical methods have been developed to understand HS-protein interactions. Also, with the advancement of CRISPR technology, genetic modification of HS-protein interactions, either by manipulating HS structure or protein structure, has become an increasingly routine tool to decipher the physiological significance of HS-protein interactions. The aim of the current Research Topic is to cover recent and promising research trends in structural characterization of HS-protein interactions, determining the physiological significance of HS-protein interactions, and pharmacological manipulation of HS-protein interactions.
Areas to be covered in this Research Topic may include, but are not limited to:
• Genetic manipulation of HS-protein interactions in vivo
• Novel methods of characterization of HS-protein interactions
• HS interactome
• Therapeutics strategies targeting HS-protein interactions
• Characterization of novel HS-binding proteins
• Structure of HS-protein complex
• Identification of HS-binding site
Universally expressed by all mammalian cells, heparan sulfate (HS) is a major and often dominant component of the landscape at the cell surface and thus plays essential roles in cell signaling and cell-cell interactions. At the cell surface and in the extracellular matrix, HS exerts its biological functions by interacting with hundreds of HS-binding proteins, which include growth factors, chemokines, cytokines, coagulation factors, complements, enzymes, enzyme inhibitors, transmembrane receptors, decoy receptors, adhesion molecules, and matrix proteins. One unique feature of HS-binding proteins is they are structurally highly diverse because HS-binding capability can arise from almost any protein fold. Understanding the structural basis of HS-protein interaction is often the key to elucidating the physiological significance of a particular HS-protein interaction.
It is apparent that without a sophisticated understanding of the structural basis of particular HS-protein interactions, it is difficult to gain any significant insight on how HS regulates the pathophysiological roles of the HS-binding protein in question. Such insight is also critical if one desires to alter the biological functions of HS-binding proteins by manipulating HS-protein interactions. In the past decade, many new biophysical and biochemical methods have been developed to understand HS-protein interactions. Also, with the advancement of CRISPR technology, genetic modification of HS-protein interactions, either by manipulating HS structure or protein structure, has become an increasingly routine tool to decipher the physiological significance of HS-protein interactions. The aim of the current Research Topic is to cover recent and promising research trends in structural characterization of HS-protein interactions, determining the physiological significance of HS-protein interactions, and pharmacological manipulation of HS-protein interactions.
Areas to be covered in this Research Topic may include, but are not limited to:
• Genetic manipulation of HS-protein interactions in vivo
• Novel methods of characterization of HS-protein interactions
• HS interactome
• Therapeutics strategies targeting HS-protein interactions
• Characterization of novel HS-binding proteins
• Structure of HS-protein complex
• Identification of HS-binding site