4n4c

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Crystal structure of the C-terminal swapped dimer of a Bovine seminal ribonuclease mutant

Structural highlights

4n4c is a 2 chain structure with sequence from Bos taurus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.48Å
Ligands:PO4, YCM
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RNS_BOVIN This enzyme hydrolyzes both single- and double-stranded RNA.

Publication Abstract from PubMed

Bovine seminal ribonuclease (BS-RNase) acquires an interesting anti-tumor activity associated with the swapping on the N-termini. 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.

The multiple forms of Bovine Seminal Ribonuclease: structure and stability of a C-terminal swapped dimer.,Sica F, Pica A, Merlino A, Krauss IR, Ercole C, Picone D FEBS Lett. 2013 Oct 15. pii: S0014-5793(13)00745-X. doi:, 10.1016/j.febslet.2013.10.003. PMID:24140346[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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Citations
1 reviews cite this structure
Biological Activities of Secretory RNases: Focus on Their Oligomerization to Design Antitumor Drugs.
Gotte et al. (2019)
0 more
3 other articles
No citations found

See Also

References

  1. ↑ Sica F, Pica A, Merlino A, Krauss IR, Ercole C, Picone D. The multiple forms of Bovine Seminal Ribonuclease: structure and stability of a C-terminal swapped dimer. FEBS Lett. 2013 Oct 15. pii: S0014-5793(13)00745-X. doi:, 10.1016/j.febslet.2013.10.003. PMID:24140346 doi:http://dx.doi.org/10.1016/j.febslet.2013.10.003

Contents


PDB ID 4n4c

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