{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Stolz M"],"funding":["European Research Council"],"pagination":["eaea7735"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12758552"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["12(1)"],"pubmed_abstract":["Adaptive immunity depends on major histocompatibility complex class I (MHC I) presentation of peptides, a process orchestrated by the peptide-loading complex (PLC) in the endoplasmic reticulum (ER). The PLC ensures precise peptide selection and loading and is a major target of viral immune evasion, notably by human cytomegalovirus (HCMV). Here, we report the 2.59- to 2.88-Å cryo-electron microscopy structure of native human PLC bound to the HCMV immune evasin US6. US6 inhibits the transporter associated with antigen processing 1/2 (TAP1/2) by laterally attaching its transmembrane helix to TAP2 using a disulfide-rich domain to mimic a translocating peptide. This domain blocks the ER-lumenal exit and locks TAP in an outward-facing conformation with closed nucleotide-binding domains and asymm"],"journal":["Science advances"],"pubmed_title":["Architectural principles of transporter-chaperone coupling within the native MHC I peptide-loading complex."],"pmcid":["PMC12758552"],"funding_grant_id":["101141396"],"pubmed_authors":["Susac L","Tampe R","Keller R","Saggau L","Fahim A","Mancia F","Trowitzsch S","Stolz M"],"additional_accession":[]},"is_claimable":false,"name":"Architectural principles of transporter-chaperone coupling within the native MHC I peptide-loading complex.","description":"Adaptive immunity depends on major histocompatibility complex class I (MHC I) presentation of peptides, a process orchestrated by the peptide-loading complex (PLC) in the endoplasmic reticulum (ER). The PLC ensures precise peptide selection and loading and is a major target of viral immune evasion, notably by human cytomegalovirus (HCMV). Here, we report the 2.59- to 2.88-Å cryo-electron microscopy structure of native human PLC bound to the HCMV immune evasin US6. US6 inhibits the transporter associated with antigen processing 1/2 (TAP1/2) by laterally attaching its transmembrane helix to TAP2 using a disulfide-rich domain to mimic a translocating peptide. This domain blocks the ER-lumenal exit and locks TAP in an outward-facing conformation with closed nucleotide-binding domains and asymm","dates":{"release":"2026-01-01T00:00:00Z","publication":"2026 Jan","modification":"2026-06-09T05:15:46.02Z","creation":"2026-06-09T03:07:29.488Z"},"accession":"S-EPMC12758552","cross_references":{"pubmed":["41481733"],"doi":["10.1126/sciadv.aea7735"]}}