Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The structure of the cold-shock domain protein from Neisseria meningitidis has been solved to 2.6 A resolution and shown to comprise a dimer formed by the exchange of two beta-strands between protein monomers. The overall fold of the monomer closely resembles those of other bacterial cold-shock proteins. The neisserial protein behaved as a monomer in solution and was shown to bind to a hexathymidine oligonucleotide with a stoichiometry of 1:1 and a K(d) of 1.25 microM.
Structure of the cold-shock domain protein from Neisseria meningitidis reveals a strand-exchanged dimer.,Ren J, Nettleship JE, Sainsbury S, Saunders NJ, Owens RJ Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Apr 1;64(Pt, 4):247-51. Epub 2008 Mar 21. PMID:18391418[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ren J, Nettleship JE, Sainsbury S, Saunders NJ, Owens RJ. Structure of the cold-shock domain protein from Neisseria meningitidis reveals a strand-exchanged dimer. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Apr 1;64(Pt, 4):247-51. Epub 2008 Mar 21. PMID:18391418 doi:10.1107/S1744309108005411
