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The multiple forms of bovine seminal ribonuclease: Structure and stability of a C‐terminal swapped dimer
Author(s) -
Sica Filomena,
Pica Andrea,
Merlino Antonello,
Russo Krauss Irene,
Ercole Carmine,
Picone Delia
Publication year - 2013
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2013.10.003
Subject(s) - dimer , rnase p , ribonuclease , chemistry , protein quaternary structure , s tag , stereochemistry , monomer , peptide , dissociation (chemistry) , rnase h , crystallography , protein subunit , biochemistry , rna , gene , organic chemistry , polymer
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.