Reconstitution of peptide‐binding activity by TAP in proteoliposomes

FEBS Letters

Androlewicz, Matthew J.¹  Stephens, David B.¹ 

[1] Immunology Program, H. Lee Moffitt Cancer Center and Research Institute, and the Department of Biochemistry and Molecular Biology, University of South Florida College of Medicine, 12902 Magnolia Dr., Tampa, FL 33612, USA

关键词: TAP;    Reconstitution;    Antigen processing;    Proteoliposome;    ABC;    ATP-binding cassette;    CHAPS;    3-[(3-cholamidopropyl)dimethylammonio]-1-propane-sulfonate;    HSAB;    N-hydroxysuccinimidyl-4-azidobenzoate;    MHC;    major histocompatibility complex;    NOG;    n-octyl glucoside;    TAP;    transporter associated with antigen processing;    TX-100;    Triton X-100;   

DOI  :  10.1016/S0014-5793(97)01221-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The purification and functional reconstitution of the transporter associated with antigen processing (TAP) is crucial for a complete molecular understanding of its action. Here, we report the conditions for the successful solubilization of human TAP from cellular membranes while maintaining TAP peptide-binding activity. In addition, solubilized TAP was incorporated into proteoliposomes and shown to possess specific peptide-binding activity. These studies provide the foundation for future attempts to achieve the complete functional reconstitution of TAP, which includes peptide transport.

【 授权许可】

Unknown