The human cytomegalovirus gene product US6 inhibits ATP binding by TAP

EMBO Journal

Volumn 20, Issue 3, 2001, Pages 387-396

  Hewitt, E W ^a   Gupta, S S ^a   Lehner, P J ^a  

^a ADDENBROOKE S HOSPITAL   (United Kingdom)

Author keywords

ABC transporter; Antigen presentation; Human cytomegalovirus; TAP; US6

Indexed keywords

ABC TRANSPORTER; ADENOSINE TRIPHOSPHATE; GENE PRODUCT; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; PROTEIN US6; TRANSPORTER ASSOCIATED WITH ANTIGEN PROCESSING 1; UNCLASSIFIED DRUG;

ANTIGEN EXPRESSION; ANTIGEN PRESENTATION; ANTIGEN RECOGNITION; ARTICLE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; CYTOTOXIC T LYMPHOCYTE; ENDOPLASMIC RETICULUM; FLOW CYTOMETRY; GENE INDUCTION; GENE TRANSLOCATION; HELA CELL; HUMAN; HUMAN CELL; HUMAN CYTOMEGALOVIRUS; IMMUNOBLOTTING; PRIORITY JOURNAL; PROTEIN ASSEMBLY; THERMOSTABILITY;

ADENOSINE TRIPHOSPHATE; AFFINITY LABELS; ANTIGEN PRESENTATION; ATP-BINDING CASSETTE TRANSPORTERS; BASE SEQUENCE; BINDING SITES; CELL LINE; CYTOMEGALOVIRUS; DRUG STABILITY; HELA CELLS; HISTOCOMPATIBILITY ANTIGENS CLASS I; HUMANS; OLIGONUCLEOTIDE PROBES; PROTEIN CONFORMATION; VIRAL ENVELOPE PROTEINS;

ANIMALIA; DNA VIRUSES; HUMAN HERPESVIRUS 5;

EID: 0035253873     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/20.3.387     Document Type: Article

References (46)

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3. The ER-luminal domain of the HCMV glycoprotein US6 inhibits peptide translocation by TAP
4. Partial purification and reconstitution of the human multidrug-resistance pump: Characterization of the drug-stimulatable ATP hydrolysis
5. Human transporters associated with antigen processing possess a promiscuous peptidebinding site
6. Characteristics of peptide and major histocompatibility complex class I/β2-microglobulin binding to the transporters associated with antigen processing (TAP1 and TAP2)
7. Transport into and out of the Golgi complex studied by transfecting cells with cDNAs encoding horseradish peroxidase
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9. Splice acceptor site mutation of the transporter associated with antigen processing-1 gene in human bare lymphocyte syndrome
10. The active site of ICP47, a herpes simplex virus-encoded inhibitor of the major histocompatibility complex (MHC)-encoded peptide transporter associated with antigen processing (TAP), maps to the NH2-terminal 35 residues
11. A viral ER-resident glycoprotein inactivates the MHC-encoded peptide transporter
12. Herpes simplex virus turns off the TAP to evade host immunity
13. ABC-ATPases, adaptable energy generators fuelling transmembrane movement of a variety of molecules in organisms from bacteria to humans
14. Assembly and function of the two ABC transporter proteins encoded in the human major histocompatibility complex
15. Nucleotide binding by TAP mediates association with peptide and release of assembled MHC class I molecules
16. Translocation of long peptides by transporters associated with antigen processing (TAP)
17. The immunoevasive function encoded by the mouse cytomegalovirus gene m152 protects the virus against T cell control in vivo
18. Herpes simplex virus inhibitor ICP47 destabilizes the transporter associated with antigen processing (TAP) heterodimer
19. Pairing of the nucleotide binding domains of the transporter associated with antigen processing
20. Antigen presentation: Coming out gracefully
21. The human cytomegalovirus US6 glycoprotein inhibits transporter associated with antigen processing-dependent peptide translocation
22. P-glycoprotein function involves conformational transitions detectable by differential immunoreactivity
23. Functional expression and purification of the ABC transporter complex associated with antigen processing (TAP) in insect cells
24. Nucleotide binding to the hydrophilic C-terminal domain of the transporter associated with antigen processing (TAP)
25. Selective and ATP-dependent translocation of peptides by the MHC-encoded transporter
26. Kinetic analysis of peptide binding to the TAP transport complex: Evidence for structural rearrangements induced by substrate binding
27. Multiple regions of the transporter associated with antigen processing (TAP) contribute to its peptide binding site
28. Identification of a contact region for peptide on the TAP1 chain of the transporter associated with antigen processing
29. MHC class I/β2-microglobulin complexes associate with TAP transporters before peptide binding
30. A critical role for tapasin in the assembly and function of multimeric MHC class I-TAP complexes
31. Mechanisms of MHC class I-restricted antigen processing
32. Use of a monoclonal antibody (W6/32) in structural studies of HLA-A,B,C, antigens
33. The major substrates for TAP in vivo are derived from newly synthesized proteins
34. Assembly, intracellular localization and nucleotide binding properties of the human peptide transporters TAP1 and TAP2 expressed by recombinant vaccinia viruses
35. Roles for calreticulin and a novel glycoprotein, tapasin, in the interaction of MHC class I molecules with TAP
36. Expression of the human multidrug resistance cDNA in insect cells generates a high activity drug-stimulated membrane ATPase
37. ATP-binding-cassette (ABC) transport systems: Functional and structural aspects of the ATP-hydrolyzing subunits/domains
38. Functional reconstitution of drug transport and ATPase activity in proteoliposomes containing partially purified P-glycoprotein
39. Monoclonal antibodies raised against denatured HLA-B locus heavy chains permit biochemical characterization of certain HLA-C locus products
40. Inhibition of MHC class I-restricted antigen presentation by Υ2-herpesviruses
41. Stable binding of the herpes simplex virus ICP47 protein to the peptide binding site of TAP
42. Viral subversion of the immune system
43. Role of nucleotides and peptide substrate for stability and functional state of the human ABC family transporters associated with antigen processing
44. A sequential model for peptide binding and transport by the transporters associated with antigen processing
45. Membrane topology and dimerization of the two subunits of the transporter associated with antigen processing reveal a three-domain structure
46. Head-head/ tail-tail relative orientation of the pore-forming domains of the heterodimeric ABC transporter TAP