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  Peptide binding and photo-crosslinking to detergent solubilized and to reconstituted transporter associated with antigen processing (tap)

Uebel, S., Plantinga, T., Weber, P. J. A., Becksickinger, A. G., & Tampe, R. (1997). Peptide binding and photo-crosslinking to detergent solubilized and to reconstituted transporter associated with antigen processing (tap). FEBS Letters, 416(3), 359-363.

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 Creators:
Uebel, S.1, Author              
Plantinga, T.1, Author              
Weber, P. J. A., Author
Becksickinger, A. G., Author
Tampe, R.2, Author
Affiliations:
1Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565142              
2External Organizations, ou_persistent22              

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Free keywords: Abc transporter; Solubilization; Reconstitution; Membrane protein; Photo-crosslinking.; Major histocompatibility complex; Class-ii region; Endoplasmic-reticulum; Rma-s; Mhc; Proteins; Gene; Translocation; Expression; Molecules.; Biochemistry & biophysics.
 Abstract: The transporter associated with antigen processing (TAP) is essential for peptide loading onto major histocompatibility (MHC) class I molecules by translocating peptides into the endoplasmic reticulum. We have explored the conditions for detergent solubilization of functionally active, heterologously expressed human TAP from microsomal membranes, The efficiency to solubilize TAP was tested for a variety of detergents as well as for different solubilization conditions, The activity of the solubilized TAP complex mas analyzed over time, using a non-radioactive crosslinking assay,vith a photo-activateable peptide, in the presence or absence of external lipid, The detergent CHAPS mas found optimally to retain activity and thus allowed us to reconstitute detergent-solubilized, active TAP into proteoliposomes. (C) 1997 Federation of European Biochemical Societies. [References: 35]

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 Dates: 1997-10-27
 Publication Status: Published in print
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 Rev. Type: -
 Identifiers: eDoc: 318410
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Title: FEBS Letters
Source Genre: Journal
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Pages: - Volume / Issue: 416 (3) Sequence Number: - Start / End Page: 359 - 363 Identifier: -