Small heat shock proteins (sHsps) are molecular chaperones which are induced under stress conditions such as oxidative, heat, acidic etc., and prevent the aggregation/mis-folding of various client proteins which are prone to partial denaturation. sHsps are generally the first line of defense against stress and exhibit holdase/chaperone function. They are found in almost all organisms and are characterized by a signature stretch of amino acid residues known as the a-crystallin domain, which is flanked by the N-terminal and C-terminal regions/domains. These three regions play an important role in substrate binding, maintaining the oligomeric assembly, and the chaperone function of sHsps. Mutations, stresses, and post-translational modifications (PTMs) of sHsps are found in various human diseases that often modulates the structure, substrate binding capability, subunit exchange dynamics, and chaperone function of sHsps. Therefore, understanding the structure-function relationship of sHsps with diseases will provide new avenues for building better therapeutics and drugs by targeting the sHsps.
Investigating the role of structural and functional modulations of sHsps (due to mutations, stresses and PTMs) in diseases is multidisciplinary in nature. It involves intervention from the area’s molecular biology, microbiology, biophysics, cell biology, biochemistry, and bioengineering. The structure-function correlation of lens sHsps with different eye diseases, especially cataracts, has been explored to significant extent under various mutations, stresses and PTMs. But such correlations between structure-function and diseases for various other sHsps are less established.
Therefore, our aim is to collate a series of original articles and reviews that address the structure-function role of sHsps in diseases. In particular, we aim to collect studies which outline the role of mutations, different stresses (especially oxidative stress), and PTMs on the structure and function of sHps and their relationship to the disease. This will expand our knowledge on the relationship between structure-function modulations of sHsps with diseases and will be a steppingstone towards the generation of new therapeutics.
We are seeking contributions in form of original articles, reviews, mini-reviews, and short communications on the following topics:
• PTMs and their effects on the structure-function of sHsps and their correlation with a particular disease
• Effect of different disease-causing stresses (especially oxidative stress) on the structure-function of sHsps
• Effect of mutations those are responsible for a particular disease on the structure, function, and substrate binding capability of sHsps
• Protein engineering of sHsps by mutagenesis to build better therapeutics.
The above list is neither exhaustive nor exclusive. Articles may be either data-based novel observations or must grant new insights into the correlation between the structure-function dynamics of sHsps with disease.
Small heat shock proteins (sHsps) are molecular chaperones which are induced under stress conditions such as oxidative, heat, acidic etc., and prevent the aggregation/mis-folding of various client proteins which are prone to partial denaturation. sHsps are generally the first line of defense against stress and exhibit holdase/chaperone function. They are found in almost all organisms and are characterized by a signature stretch of amino acid residues known as the a-crystallin domain, which is flanked by the N-terminal and C-terminal regions/domains. These three regions play an important role in substrate binding, maintaining the oligomeric assembly, and the chaperone function of sHsps. Mutations, stresses, and post-translational modifications (PTMs) of sHsps are found in various human diseases that often modulates the structure, substrate binding capability, subunit exchange dynamics, and chaperone function of sHsps. Therefore, understanding the structure-function relationship of sHsps with diseases will provide new avenues for building better therapeutics and drugs by targeting the sHsps.
Investigating the role of structural and functional modulations of sHsps (due to mutations, stresses and PTMs) in diseases is multidisciplinary in nature. It involves intervention from the area’s molecular biology, microbiology, biophysics, cell biology, biochemistry, and bioengineering. The structure-function correlation of lens sHsps with different eye diseases, especially cataracts, has been explored to significant extent under various mutations, stresses and PTMs. But such correlations between structure-function and diseases for various other sHsps are less established.
Therefore, our aim is to collate a series of original articles and reviews that address the structure-function role of sHsps in diseases. In particular, we aim to collect studies which outline the role of mutations, different stresses (especially oxidative stress), and PTMs on the structure and function of sHps and their relationship to the disease. This will expand our knowledge on the relationship between structure-function modulations of sHsps with diseases and will be a steppingstone towards the generation of new therapeutics.
We are seeking contributions in form of original articles, reviews, mini-reviews, and short communications on the following topics:
• PTMs and their effects on the structure-function of sHsps and their correlation with a particular disease
• Effect of different disease-causing stresses (especially oxidative stress) on the structure-function of sHsps
• Effect of mutations those are responsible for a particular disease on the structure, function, and substrate binding capability of sHsps
• Protein engineering of sHsps by mutagenesis to build better therapeutics.
The above list is neither exhaustive nor exclusive. Articles may be either data-based novel observations or must grant new insights into the correlation between the structure-function dynamics of sHsps with disease.
