The multiple forms of bovine seminal ribonuclease: Structure and stability of a C-terminal swapped dimer(442 views) Sica F, Pica A, Merlino A, Russo Krauss I, Ercole C, Picone D
Febs Lett (ISSN: 0014-5793, 0014-5793print, 1873-3468electronic), 2013 Nov 29; 587(23): 3755-3762.
Keywords: Bovine Seminal Ribonuclease, C-Terminal 3d Domain Swapping, Cytotoxic Rnase, Hinge Peptide, Multiple Swapping, Dimer, Isoenzyme, Amino Acid Sequence, Article, Carboxy Terminal Sequence, Chemical Model, Controlled Study, Enzyme Stability, Enzyme Structure, Mutation, Nonhuman, Priority Journal, Protein Function, Protein Quaternary Structure, Seminal Plasma, X Ray, Artificial Dimer Of Bs-Rnase Obtained By Incubation In Acetic Acid Of Mbs And Lyophilisation, Artificial Dimer Of Staa-Bs-Rnase Obtained By Incubation In Acetic Acid Of Staa-Mbs And Lyophilisation, Bovine Pancreatic Ribonuclease (ec 3 1 2 27 5), Covalent Swapped Isomer Of Bs-Rnase, Covalent Unswapped Isomer Of Bs-Rnase, D(art)-Bs, D(art)-Staa-Bs, Dithiothreitol, G16s N17t P19a S20a Variant Of Bs-Rnase, G16s N17t P19a S20a Variant Of Mbs, Iodoacetamide, L28q Variant Of Mbs, L28q-Mbs, M×m, Monomeric Derivative Of Bs-Rnase With Cysteines 31 And 32 Either Linked To Glutathione Moieties Or Alkylated With Iodoacetamide, Ncd-Bs, Non-Covalent Swapped Dimer Of Bs-Rnase With Cysteines 31 And 32 Linked To Iodoacetamide, Obtained By Selective Reduction Of The Swapped Isoform And Iodoalkylation, P19a L28q Variant Of Bs-Rnase, P19a L28q Variant Of Mbs, Palq-Bs-Rnase, Palq-Mbs, R80s Variant Of Staa-Bs-Rnase, R80s Variant Of Staa-Mbs, R80s-Staa-Bs-Rnase, R80s-Staa-Mbs, Ribonuclease Inhibitor, Size-Exclusion Chromatography, Animals, Cattle, Crystallography, X-Ray, Endoribonucleases, Molecular Sequence Data, Protein Multimerization, Protein Structure, Tertiary, D (art)-Bs, D (art)-Staa-Bs,
Affiliations: *** IBB - CNR ***
Department of Chemical Sciences, University of Naples 'Federico II', via Cintia, 80126 Naples, Italy
Institute of Biostructures and Bioimaging, CNR, Via Mezzocannone 16, 80134 Naples, Italy
National Institute Biostructures and Biosystems, Inter-University Consortium, Viale Medaglie d'Oro 305, I-00136 Rome, Italy
References: Not available.
The multiple forms of bovine seminal ribonuclease: Structure and stability of a C-terminal swapped dimer
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. Structure summary of protein interactions: BS-RNase and BS-RNase bind by x-ray crystallography (View interaction) BS-RNase and BS-RNase bind by molecular sieving (1, 2) BS-RNase and BS-RNase bind by blue native page (View interaction) (C) 2013 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
The multiple forms of bovine seminal ribonuclease: Structure and stability of a C-terminal swapped dimer
No results.
The multiple forms of bovine seminal ribonuclease: Structure and stability of a C-terminal swapped dimer