Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10870807 | FEBS Letters | 2013 | 8 Pages |
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.
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Authors
Giovanni Gotte, Douglas V. Laurents, Antonello Merlino, Delia Picone, Roberta Spadaccini,