The multiple forms of bovine seminal ribonuclease: Structure and stability of a C-terminal swapped dimer
| Autor: | Delia Picone, Andrea Pica, Filomena Sica, Antonello Merlino, Irene Russo Krauss, Carmine Ercole |
|---|---|
| Přispěvatelé: | Sica, Filomena, Pica, Andrea, Merlino, Antonello, RUSSO KRAUSS, Irene, Ercole, Carmine, Picone, Delia |
| Rok vydání: | 2013 |
| Předmět: |
Multiple swapping
RNase P Stereochemistry C-terminal 3D domain swapping Dimer Ribonuclease inhibitor Molecular Sequence Data Size-exclusion chromatography Biophysics Peptide Hinge peptide Crystallography X-Ray Biochemistry chemistry.chemical_compound Structural Biology Endoribonucleases Hydrolase Genetics Animals Amino Acid Sequence Protein Structure Quaternary Molecular Biology chemistry.chemical_classification Cell Biology Domain swapping Protein Structure Tertiary chemistry Mutation Iodoacetamide Bovine seminal ribonuclease Cattle Protein quaternary structure Protein Multimerization Cytotoxic RNase |
| Zdroj: | FEBS Letters. 587:3755-3762 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/j.febslet.2013.10.003 |
| Popis: | Bovine seminal ribonuclease (BS-RNase) acquires an interesting anti-tumor activity associated with the swapping on the N-terminal. The first direct experimental evidence on the formation of a C-terminal swapped dimer (C-dimer) obtained from the monomeric derivative of BS-RNase, although under non-native conditions, is here reported. The X-ray model of this dimer reveals a quaternary structure different from that of the C-dimer of RNase A, due to the presence of three mutations in the hinge peptide 111–116. The mutations increase the hinge peptide flexibility and decrease the stability of the C-dimer against dissociation. The biological implications of the structural data are also discussed. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Plný text