Structural and functional relationships of natural and artificial dimeric bovine ribonucleases: New scaffolds for potential antitumor drugs

Gotte, Giovanni; Laurents, Douglas V.; Antonello, Merlino; Delia, Picone; Roberta, Spadaccini

doi:10.1016/j.febslet.2013.09.038

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.

Titolo:	Structural and functional relationships of natural and artificial dimeric bovine ribonucleases: New scaffolds for potential antitumor drugs
Autori:	GOTTE, Giovanni Douglas V. Laurents Antonello Merlino Delia Picone Roberta Spadaccini mostra contributor esterni nascondi contributor esterni
Data di pubblicazione:	2013
Rivista:	FEBS LETTERS
Handle:	http://hdl.handle.net/11562/653971
Appare nelle tipologie:	01.01 Articolo in Rivista

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http://hdl.handle.net/11562/653971

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