Structural and functional relationships of natural and artificial dimeric bovine ribonucleases: New scaffolds for potential antitumor drugs. Issue 22 (7th October 2013)

• Record Type: Journal Article
• Authors: Gotte, Giovanni; Laurents, Douglas V.; Merlino, Antonello; Picone, Delia; Spadaccini, Roberta
• Is Part Of: FEBS letters. Volume 587:Issue 22(2013)
• Page Start: 3601
• Page End: 3608
• Publication Date: 2013-10-07
• Subjects: Ribonuclease A -- Dimeric RNase -- Antitumor RNase -- Bovine seminal ribonuclease -- Protein aggregation -- 3D-domain swapping; Biochemistry -- Periodicals; Biophysics -- Periodicals; Molecular biology -- Periodicals; Biochimie -- Périodiques; Biochemistry; Biophysics; Molecular biology; Periodicals; 572.05
• DOI: 10.1016/j.febslet.2013.09.038
• Languages: English
• ISSNs: 0014-5793

Abstract

Abstract : Protein aggregation via 3D domain swapping is a complex mechanism which can lead to the acquisition of new biological, benign or also malignant functions, such as amyloid deposits. In this context, RNase A represents a fascinating model system, since by dislocating different polypeptide chain regions, it forms many diverse oligomers. No other protein displays such a large number of different quaternary structures. Here we report a comparative structural analysis between natural and artificial RNase A dimers and bovine seminal ribonuclease, a natively dimeric RNase with antitumor activity, with the aim to design RNase A derivatives with improved pharmacological potential.