Solution structure and dynamics of S100A5 in the apo and Ca2+-bound states
| Autor: | Giacomo Parigi, Jing Yuan, Claudio Luchinat, Ivano Bertini, Tilemachos Karavelas, Soumyasri Das Gupta, Xiaoyu Hu |
|---|---|
| Rok vydání: | 2009 |
| Předmět: |
Models
Molecular Surface Properties Stereochemistry Protein subunit Static Electricity chemistry.chemical_element Calcium Biochemistry S100 protein Inorganic Chemistry Glycation Calcium-binding protein Humans Protein Interaction Domains and Motifs EF Hand Motifs Protein Structure Quaternary Receptor Nuclear Magnetic Resonance Biomolecular Carbon Isotopes Principal Component Analysis Nitrogen Isotopes Chemistry Protein dynamics S100 Proteins Numerical Analysis Computer-Assisted Recombinant Proteins Protein Multimerization Apoproteins Algorithms Binding domain |
| Zdroj: | JBIC Journal of Biological Inorganic Chemistry. 14:1097-1107 |
| ISSN: | 1432-1327 0949-8257 |
| DOI: | 10.1007/s00775-009-0553-1 |
| Popis: | S100A5 is a calcium binding protein of the S100 family, with one canonical and one S100-specific EF-hand motif per subunit. Although its function is still unknown, it has recently been reported to be one of the S100 proteins able to interact with the receptor for advanced glycation end products. The homodimeric solution structures of S100A5 in both the apo and the calcium(II)-loaded forms have been obtained, and show a conformational rearrangement upon calcium binding. This rearrangement involves, in particular, the hinge loop connecting the N-terminal and the C-terminal EF-hand domains, the reorientation of helix III with respect to helix IV, as common to several S100 proteins, and the elongation of helix IV. The details of the structural changes are important because they must be related to the different functions, still largely unknown, of the different members of the S100 family. For the first time for a full-length S100 protein, relaxation measurements were performed on both the apo and the calcium-bound forms. A quite large mobility was observed in the hinge loop, which is not quenched in the calcium form. The structural differences resulting upon calcium binding change the global shape and the distribution of hydrophobic and charged residues of the S100A5 homodimer in a modest but significantly different manner with respect to the closest homologues S100A4 and S100A6. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|