Abstract
Small heat shock proteins (sHsp) form a large ubiquitous family of proteins expressed in all phyla of living organisms. The members of this family have low molecular masses (13-43 kDa) and contain a conservative α-crystallin domain. This domain (about 90 residues) consists of several β-strands forming two β-sheets packed in immunoglobulinlike manner. The α-crystallin domain plays an important role in formation of stable sHsp dimers, which are the building blocks of the large sHsp oligomers. A large N-terminal domain and a short C-terminal extension flank the α-crystallin domain. Both the N-terminal domain and the C-terminal extension are flexible, susceptible to proteolysis, prone to posttranslational modifications, and are predominantly intrinsically disordered. Differently oriented N-terminal domains interact with each other, with the core α-crystallin domain of the same or neighboring dimers and play important role in formation of large sHsp oligomers. Phosphorylation of certain sites in the N-terminal domain affects the sHsp quaternary structure, the sHsp interaction with target proteins and the sHsp chaperone-like activity. The C-terminal extension often carrying the conservative tripeptide (I/V/L)-X-(I/V/L) is capable of binding to a hydrophobic groove on the surface of the core α-crystallin domain of neighboring dimer, thus affecting the plasticity and the overall structure of sHsp oligomers. The Cterminal extension interacts with target proteins and affects their interaction with the α-crystallin domain increasing solubility of the complexes formed by sHsp and their targets. Thus, disordered N- and C-terminal sequences play important role in the structure, regulation and functioning of sHsp.
Keywords: Intrinsic disorder, protein-protein interaction, phosphorylation, small heat shock proteins, sHsp, DNAJ, axonopodis, Methanococcus jannaschii, Xanthomonas, HspA
Current Protein & Peptide Science
Title: The Role of Intrinsically Disordered Regions in the Structure and Functioning of Small Heat Shock Proteins
Volume: 13 Issue: 1
Author(s): Maria V. Sudnitsyna, Evgeny V. Mymrikov, Alim S. Seit-Nebi and Nikolai B. Gusev
Affiliation:
Keywords: Intrinsic disorder, protein-protein interaction, phosphorylation, small heat shock proteins, sHsp, DNAJ, axonopodis, Methanococcus jannaschii, Xanthomonas, HspA
Abstract: Small heat shock proteins (sHsp) form a large ubiquitous family of proteins expressed in all phyla of living organisms. The members of this family have low molecular masses (13-43 kDa) and contain a conservative α-crystallin domain. This domain (about 90 residues) consists of several β-strands forming two β-sheets packed in immunoglobulinlike manner. The α-crystallin domain plays an important role in formation of stable sHsp dimers, which are the building blocks of the large sHsp oligomers. A large N-terminal domain and a short C-terminal extension flank the α-crystallin domain. Both the N-terminal domain and the C-terminal extension are flexible, susceptible to proteolysis, prone to posttranslational modifications, and are predominantly intrinsically disordered. Differently oriented N-terminal domains interact with each other, with the core α-crystallin domain of the same or neighboring dimers and play important role in formation of large sHsp oligomers. Phosphorylation of certain sites in the N-terminal domain affects the sHsp quaternary structure, the sHsp interaction with target proteins and the sHsp chaperone-like activity. The C-terminal extension often carrying the conservative tripeptide (I/V/L)-X-(I/V/L) is capable of binding to a hydrophobic groove on the surface of the core α-crystallin domain of neighboring dimer, thus affecting the plasticity and the overall structure of sHsp oligomers. The Cterminal extension interacts with target proteins and affects their interaction with the α-crystallin domain increasing solubility of the complexes formed by sHsp and their targets. Thus, disordered N- and C-terminal sequences play important role in the structure, regulation and functioning of sHsp.
Export Options
About this article
Cite this article as:
V. Sudnitsyna Maria, V. Mymrikov Evgeny, S. Seit-Nebi Alim and B. Gusev Nikolai, The Role of Intrinsically Disordered Regions in the Structure and Functioning of Small Heat Shock Proteins, Current Protein & Peptide Science 2012; 13 (1) . https://dx.doi.org/10.2174/138920312799277875
DOI https://dx.doi.org/10.2174/138920312799277875 |
Print ISSN 1389-2037 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5550 |
Call for Papers in Thematic Issues
Advancements in Proteomic and Peptidomic Approaches in Cancer Immunotherapy: Unveiling the Immune Microenvironment
The scope of this thematic issue centers on the integration of proteomic and peptidomic technologies into the field of cancer immunotherapy, with a particular emphasis on exploring the tumor immune microenvironment. This issue aims to gather contributions that illustrate the application of these advanced methodologies in unveiling the complex interplay ...read more
Artificial Intelligence for Protein Research
Protein research, essential for understanding biological processes and creating therapeutics, faces challenges due to the intricate nature of protein structures and functions. Traditional methods are limited in exploring the vast protein sequence space efficiently. Artificial intelligence (AI) and machine learning (ML) offer promising solutions by improving predictions and speeding up ...read more
Nutrition and Metabolism in Musculoskeletal Diseases
The musculoskeletal system consists mainly of cartilage, bone, muscles, tendons, connective tissue and ligaments. Balanced metabolism is of vital importance for the homeostasis of the musculoskeletal system. A series of musculoskeletal diseases (for example, sarcopenia, osteoporosis) are resulted from the dysregulated metabolism of the musculoskeletal system. Furthermore, metabolic diseases (such ...read more
Protein Folding, Aggregation and Liquid-Liquid Phase Separation
Protein folding, misfolding and aggregation remain one of the main problems of interdisciplinary science not only because many questions are still open, but also because they are important from the point of view of practical application. Protein aggregation and formation of fibrillar structures, for example, is a hallmark of a ...read more
Related Journals
- Author Guidelines
- Graphical Abstracts
- Fabricating and Stating False Information
- Research Misconduct
- Post Publication Discussions and Corrections
- Publishing Ethics and Rectitude
- Increase Visibility of Your Article
- Archiving Policies
- Peer Review Workflow
- Order Your Article Before Print
- Promote Your Article
- Manuscript Transfer Facility
- Editorial Policies
- Allegations from Whistleblowers
Related Articles
-
Solid Lipid Nanoparticles (SLNs) as a Rising Tool in Drug Delivery Science: One Step Up in Nanotechnology
Current Nanoscience Inflammasome Signaling in Pathogenesis of Lung Diseases
Current Pharmaceutical Design Extending the Clinical Horizons of Mucosal Bacterial Vaccines: Current Evidence and Future Prospects
Current Drug Targets Genomic and Pharmacogenomic Biomarkers of Parkinson’s Disease
Current Drug Metabolism Glyconanoparticles for Biomedical Applications
Combinatorial Chemistry & High Throughput Screening Adeno-Associated Viral Vector Mediated Expression of Broadly- Neutralizing Antibodies Against HIV-Hitting a Fast-Moving Target
Current HIV Research Smart pH-responsive Co-polymeric Hydrogels for Controlled Delivery of Capecitabine: Fabrication, Optimization and In Vivo Toxicology Screening
Current Drug Delivery Microdialysis in Drug Discovery
Current Drug Discovery Technologies Disorders of Sex Development: A Review
Current Women`s Health Reviews Progress of HDAC Inhibitor Panobinostat in the Treatment of Cancer
Current Drug Targets Biomedical Data Integration in Computational Drug Design and Bioinformatics
Current Computer-Aided Drug Design Personalized Medicine, Bioethics and Social Responsibilities: Re-thinking the Pharmaceutical Industry to Remedy Inequities in Patient Care and International Health
Current Pharmacogenomics and Personalized Medicine Annexin A5 Imaging: An Academic Research – Clinical Trials and Theses
Current Molecular Imaging (Discontinued) Fork Head Transcription Factors
Current Genomics Better Antiretroviral Central Nervous System Penetration is Not Associated with Reduced Chronic Pain in People Living with Human Immunodeficiency Virus
Anti-Infective Agents An Image-Based Biosensor Assay Strategy to Screen for Modulators of the microRNA 21 Biogenesis Pathway
Combinatorial Chemistry & High Throughput Screening Macronutrient Intake and Distribution in the Etiology, Prevention and Treatment of Osteosarcopenic Obesity
Current Aging Science Possibility of Enhanced Risk of Retinal Angiogenesis in Athletes with Pre- Existing Retinal Situation Abusing Erythropoietin Doping: A Hypothesis
Current Drug Safety Anticancer Antioxidant Regulatory Functions of Phytochemicals
Current Medicinal Chemistry Recent Advances and Patents on Solid Lipid Nanoparticles
Recent Patents on Drug Delivery & Formulation