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PDBsum entry 5vue

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protein ligands Protein-protein interface(s) links
Immune system PDB id
5vue

 

 

 

 

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Contents
Protein chains
276 a.a.
97 a.a.
Ligands
LEU-THR-VAL-GLN-
VAL-ALA-ARG-VAL-
TRP
Waters ×533
PDB id:
5vue
Name: Immune system
Title: Hla-b 57:01 Presenting ltvqvarvw
Structure: Hla class i histocompatibility antigen, b-57 alpha chain. Chain: a. Synonym: bw-57,mhc class i antigen b 57. Engineered: yes. Beta-2-microglobulin. Chain: b. Engineered: yes. Nonamer peptide: leu-thr-val-gln-val-ala-arg-val-trp. Chain: c.
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: hla-b, hlab. Expressed in: escherichia coli. Expression_system_taxid: 511693. Gene: b2m, cdabp0092, hdcma22p. Synthetic: yes. Synthetic construct.
Resolution:
1.80Å     R-factor:   0.168     R-free:   0.207
Authors: P.Pymm,J.Rossjohn,J.P.Vivian
Key ref: P.T.Illing et al. (2018). HLA-B57 micropolymorphism defines the sequence and conformational breadth of the immunopeptidome. Nat Commun, 9, 4693. PubMed id: 30410026 DOI: 10.1038/s41467-018-07109-w
Date:
19-May-17     Release date:   03-Oct-18    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P01889  (1B07_HUMAN) -  HLA class I histocompatibility antigen, B alpha chain from Homo sapiens
Seq:
Struc:
362 a.a.
276 a.a.*
Protein chain
Pfam   ArchSchema ?
P61769  (B2MG_HUMAN) -  Beta-2-microglobulin from Homo sapiens
Seq:
Struc:
119 a.a.
97 a.a.
Key:    PfamA domain  Secondary structure
* PDB and UniProt seqs differ at 28 residue positions (black crosses)

 

 
DOI no: 10.1038/s41467-018-07109-w Nat Commun 9:4693 (2018)
PubMed id: 30410026  
 
 
HLA-B57 micropolymorphism defines the sequence and conformational breadth of the immunopeptidome.
P.T.Illing, P.Pymm, N.P.Croft, H.G.Hilton, V.Jojic, A.S.Han, J.L.Mendoza, N.A.Mifsud, N.L.Dudek, J.McCluskey, P.Parham, J.Rossjohn, J.P.Vivian, A.W.Purcell.
 
  ABSTRACT  
 
Immunophenotypic differences between closely related human leukocyte antigen (HLA) alleles have been associated with divergent clinical outcomes in infection, autoimmunity, transplantation and drug hypersensitivity. Here we explore the impact of micropolymorphism on peptide antigen presentation by three closely related HLA molecules, HLA-B*57:01, HLA-B*57:03 and HLA-B*58:01, that are differentially associated with the HIV elite controller phenotype and adverse drug reactions. For each allotype, we mine HLA ligand data sets derived from the same parental cell proteome to define qualitative differences in peptide presentation using classical peptide binding motifs and an unbiased statistical approach. The peptide repertoires show marked qualitative overlap, with 982 peptides presented by all allomorphs. However, differences in peptide abundance, HLA-peptide stability, and HLA-bound conformation demonstrate that HLA micropolymorphism impacts more than simply the range of peptide ligands. These differences provide grounds for distinct immune reactivity and insights into the capacity of micropolymorphism to diversify immune outcomes.
 

 

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