Nucleotide binding by TAP mediates association with peptide and release of assembled MHC class I molecules (Q28145458)

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P Alberts

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E V Deverson

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J C Howard

A critical role for tapasin in the assembly and function of multimeric MHC class I-TAP complexes

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language of work or name

English

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publication date

23 September 1999

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published in

Current Biology

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volume

9

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issue

18

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page(s)

999-1008

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cites work

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Interaction of MHC class I molecules with the transporter associated with antigen processing

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MHC class I/beta 2-microglobulin complexes associate with TAP transporters before peptide binding

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Conformational changes induced in the MHC class I molecule by peptide and beta 2-microglobulin

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How does TAP associate with MHC class I molecules?

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Proteasome subunits encoded by the major histocompatibility complex are not essential for antigen presentation

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Major histocompatibility complex class I molecules interact with both subunits of the transporter associated with antigen processing, TAP1 and TAP2.

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Selective and ATP-dependent translocation of peptides by the MHC-encoded transporter

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Characterization of two Epstein-Barr virus epitopes restricted by HLA-B7.

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ABC Transporters: From Microorganisms to Man

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Evidence that transporters associated with antigen processing translocate a major histocompatibility complex class I-binding peptide into the endoplasmic reticulum in an ATP-dependent manner

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Assembly, Intracellular Localization, and Nucleotide Binding Properties of the Human Peptide Transporters TAP1 and TAP2 Expressed by Recombinant Vaccinia Viruses

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MHC class I molecules form ternary complexes with calnexin and TAP and undergo peptide-regulated interaction with TAP via their extracellular domains

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Role of nucleotides and peptide substrate for stability and functional state of the human ABC family transporters associated with antigen processing.

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