PDBsum entry 4n4c

Hydrolase

PDB id: 4n4c

Contents

Protein chains

124 a.a.

Ligands

PO4 ×2

Waters ×35

References listed in PDB file

Key reference

• Title: The multiple forms of bovine seminal ribonuclease: structure and stability of a c-Terminal swapped dimer.
• Authors: F.Sica, A.Pica, A.Merlino, I.Russo krauss, C.Ercole, D.Picone.
• Ref.: Febs Lett, 2013, 587, 3755-3762. [DOI no: 10.1016/j.febslet.2013.10.003]
• PubMed id: 24140346

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.