The serum albumin‐binding domain of streptococcal protein G is a three‐helical bundle: a heteronuclear NMR study

FEBS Letters

Kördel, Johan¹  Jendeberg, Lena¹  Jonasson, Per²  Nygren, Per-Åke²  Kraulis, Per J.¹  Nilsson, Björn¹  Uhlén, Mathias¹ 

[1] Department of Structural Biochemistry, Preclinical R&D, Pharmacia Biopharmaceuticals, S-112 87 Stockholm, Sweden;Department of Biochemistry and Biotechnology, Royal Institute of Technology, S-100 44 Stockholm, Sweden

关键词: Protein G (Streptococcus);    Serum albumin;    Secondary structure;    Global fold;    Three-helix bundle;    Nuclear magnetic resonance;   

DOI  :  10.1016/0014-5793(95)01452-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Streptococcal protein G (SPG) is a cell surface receptor protein with a multiple domain structure containing tandem repeats of serum albumin-binding domains (ABD) and immunoglobulin-binding domains (IgBD). In this paper, we have analysed the fold of ABD. Far-UV circular dichroism analysis of ABD indicates high helical content (56%). Based on an analysis of nuclear magnetic resonance ¹³C secondary chemical shifts, sequential and short-range NOEs, and a few key nuclear Overhauser effects, we conclude that the ABD is a three-helix bundle. The structure of the ABD is, thus, quite different from the IgBD of protein G [Gronenborn, A.M. et al. (1991) Science 253, 657–661]. This strongly suggests that the ABD and the IgBD of SPG have evolved independently from each other. However, the fold of ABD is similar to that of the IgBD of staphylococcal protein A, possibly indicating a common evolutionary ancestor, despite the lack of sequence homology.

【 授权许可】

Unknown