Construction of a divalent cell adhesive lysozyme by introducing the Arg‐Gly‐Asp sequence at two sites

FEBS Letters

Uyeda, Atsuko¹  Yamada, Takao¹  Kikuchi, Masakazu¹  Shimada, Yoshimi¹  Sugiyama, Shigeru¹ 

[1] Protein Engineering Research Institute, 6-2-3 Furuedai, Suita, Osaka 565, Japan

关键词: Human lysozyme;    Arg-Gly-Asp introduction;    Cell adhesion activity;    β-Turn conformation;    Divalent adhesive protein;    RGD;    Arg-Gly-Asp;    BHK;    baby hamster kidney;   

DOI  :  10.1016/0014-5793(95)01123-V

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

To increase the cell adhesion activity of 74RGD4, an RGDS-inserted mutant between Val⁷⁴ and Asn⁷⁵ of human lysozyme, one more site for the RGD introduction was investigated in the lysozyme molecule. We found that 47RGD4 with RGDS in place of AGDR (residues 47 to 50) in a β-turn region possesses the same level of adhesion activity as that of 74RGD4. The acceptance of the RGD introduction in the β-turn region of human lysozyme is in good agreement with recent studies on the functional conformation of RGD. We constructed (47,74)RGD4, a mutant containing RGD at two sites, by combining the N-terminal domain of 47RGD4 and the C-terminal domain of 74RGD4. The (47,74)RGD4 lysozyme, with two functional RGD sequences, exhibits even higher cell adhesion activity than that of 74RGD4 or 47RGD4.

【 授权许可】

Unknown