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Reviews citing this publication (1)
- Biological Activities of Secretory RNases: Focus on Their Oligomerization to Design Antitumor Drugs. Gotte G, Menegazzi M. Front Immunol 10 2626 (2019)
The multiple forms of bovine seminal ribonuclease: structure and stability of a C-terminal swapped dimer.
FEBS Lett 587 3755-62 (2013)
Abstract
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.