How does TAP pump peptides? Insights from DNA repair and traffic ATPases

This article presents an integral model of TAP function that visualizes how peptide and ATP drive the conformational changes required for pore opening and peptide transfer into the major histocompatibility complex (MHC) class I loading complex.

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Bibliographische Detailangaben
Veröffentlicht in:	Immunology today (Amsterdam. Regular ed.) 2000-12, Vol.21 (12), p.598-600
Hauptverfasser:	Reits, Eric A.J, Griekspoor, Alexander C, Neefjes, Jacques
Format:	Artikel
Sprache:	eng
Schlagworte:	ABC Transporters Adenosine Triphosphatases - chemistry Adenosine Triphosphate - pharmacology Adenosine Triphosphate - physiology Allosteric Regulation Allosteric Site Antigen Presentation Antigens - metabolism ATP ATP-Binding Cassette Sub-Family B Member 2 ATP-Binding Cassette Transporters - chemistry ATP-Binding Cassette Transporters - metabolism ATP-Binding Cassette, Sub-Family B, Member 3 ATPase Binding Sites Dimerization DNA Repair Histocompatibility Antigens Class I - metabolism Humans MHC class 1 Models, Immunological Models, Molecular Protein Binding Protein Conformation Protein Structure, Tertiary Signature motif Structure-Activity Relationship TAP TAP protein
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Beschreibung
Zusammenfassung:	This article presents an integral model of TAP function that visualizes how peptide and ATP drive the conformational changes required for pore opening and peptide transfer into the major histocompatibility complex (MHC) class I loading complex.
ISSN:	0167-5699
DOI:	10.1016/S0167-5699(00)01720-5