4jqx | pdb_00004jqx

HLA-B*44:03 in complex with Epstein-Barr virus BZLF1-derived peptide (residues 169-180)

spinqualitylabelsall models 4jqx, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4jqx is a 3 chain structure with sequence from Homo sapiens and Human gammaherpesvirus 4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.9Å Ligands: ACT, GOL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function BZLF1_EBVG Plays a key role in the switch from latent infection to lytic cycle producing new virions. Acts as a transcription factor, inducing early lytic cycle genes, and as a origin binding protein for genome replication. BZLF1 activates the promoter of another EBV gene (BSLF2+BMLF1) (By similarity). Publication Abstract from PubMed Class I HLAs generally present peptides of 8-10 aa in length, although it is unclear whether peptide length preferences are affected by HLA polymorphism. In this study, we investigated the CD8+ T cell response to the BZLF1 Ag of EBV, which includes overlapping sequences of different size that nevertheless conform to the binding motif of the large and abundant HLA-B*44 supertype. Whereas HLA-B*18:01+ individuals responded strongly and exclusively to the octamer peptide 173SELEIKRY180, HLA-B*44:03+ individuals responded to the atypically large dodecamer peptide 169EECDSELEIKRY180, which encompasses the octamer peptide. Moreover, the octamer peptide bound more stably to HLA-B*18:01 than did the dodecamer peptide, whereas, conversely, HLA-B*44:03 bound only the longer peptide. Furthermore, crystal structures of these viral peptide-HLA complexes showed that the Ag-binding cleft of HLA-B*18:01 was more ideally suited to bind shorter peptides, whereas HLA-B*44:03 exhibited characteristics that favored the presentation of longer peptides. Mass spectrometric identification of > 1000 naturally presented ligands revealed that HLA-B*18:01 was more biased toward presenting shorter peptides than was HLA-B*44:03. Collectively, these data highlight a mechanism through which polymorphism within an HLA class I supertype can diversify determinant selection and immune responses by varying peptide length preferences. HLA Peptide Length Preferences Control CD8+ T Cell Responses.,Rist MJ, Theodossis A, Croft NP, Neller MA, Welland A, Chen Z, Sullivan LC, Burrows JM, Miles JJ, Brennan RM, Gras S, Khanna R, Brooks AG, McCluskey J, Purcell AW, Rossjohn J, Burrows SR J Immunol. 2013 Jun 7. PMID:23749632 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Beta-2 microglobulin 3D structures MHC 3D structures MHC I 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA