Interactions between cro repressor and the model specific binding site

FEBS Letters

Chernov, B.K.¹  Kurochkin, A.V.¹  Skryabin, K.G.¹  Kirpichnikov, M.P.¹ 

[1] Institute of Molecular Biology, The USSR Academy of Sciences, V-334, Vavilov Str. 32, 117984 Moscow, USSR

关键词: cro repressor;    Protein structure;    Operator;    Specific binding;    1H NMR;    NMR;    nuclear magnetic resonance;    HPLC;    high pressure liquid chromatography;    DSS;    sodium 2;    2-dimethyl-2-silapentane-5-sulphonate;    CD;    circular dichroism;    NOE;    nuclear Overhauser enhancement;   

DOI  :  10.1016/0014-5793(84)80759-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Binding of λ phage cro repressor to the synthetic half of O_R3, the most conservative half of the specific binding sites, was investigated by proton nuclear magnetic resonance spectroscopy. It was found that the α-helical segment (27–36) of the protein was involved in specific interactions with the model binding site. The 3-dimensional structure of cro repressor does not change noticeably upon complex formation. Intercalation can be excluded as a possible means of interaction.

【 授权许可】

Unknown