TAP is an integral transmembrane protein involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum for association with MHC class I molecules. It is a heterodimer of TAP1 and TAP2, and the peptide-binding site is shared between the cytoplasmic loops of TAP1 and TAP2. TAP is inducible by interferon gamma and belongs to the ABC transporter family, MDR subfamily. TAP also acts as a molecular scaffold for the final stage of MHC class I folding, namely the binding of peptide. Nascent MHC class I molecules associate with TAP via tapasin. TAP is inhibited by the covalent attachment of herpes simplex virus ICP47 protein, which blocks the peptide-binding site of TAP. It is inhibited by human cytomegalovirus US6 glycoprotein, which binds to the lumenal side of the TAP complex and inhibits peptide translocation by specifically blocking ATP-binding to TAP and prevents the conformational rearrangement of TAP induced by peptide binding.