The first 37 residues are sufficient for dimerization of ribosomal L7/L12 protein

FEBS Letters

Sherstobaeva, N.M.¹  Budovskaya, E.V.¹  Gudkov, A.T.¹ 

[1] Institute of Protein Research, Russian Academy of Sciences, 142292 Pushchino, Moscow Region, Russian Federation

关键词: Ribosome;    L7/L12 protein;    Structure;    Function;   

DOI  :  10.1016/0014-5793(95)00564-P

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The ribosomal protein L7/L12 with the substitution of Cys³⁸ for the Val³⁸ residue was obtained and studied to test the orientation of polypeptide chains in the N-terminal region of the dimer. The results show that the L7/L12 dimer has a parallel (head-to-head) orientation of subunits and that its first 37 N-terminal residues are sufficient for dimerization.

【 授权许可】

Unknown