The Role of Intrinsically Disordered Regions in the Structure and Functioning of Small Heat Shock Proteins
| Autor: | Nikolai B. Gusev, Evgeny V. Mymrikov, Alim S. Seit-Nebi, Maria V. Sudnitsyna |
|---|---|
| Rok vydání: | 2012 |
| Předmět: |
medicine.diagnostic_test
Proteolysis Dimer fungi Cell Biology General Medicine Biology Biochemistry Heat-Shock Proteins Small Protein Structure Tertiary Structure-Activity Relationship chemistry.chemical_compound Protein structure chemistry Heat shock protein Domain (ring theory) Biophysics medicine Phosphorylation Structure–activity relationship Protein quaternary structure alpha-Crystallins Molecular Biology |
| Zdroj: | Current Protein & Peptide Science. 13:76-85 |
| ISSN: | 1389-2037 |
| DOI: | 10.2174/138920312799277875 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|