PDBsum entry 6p2f

Immune system

PDB id: 6p2f

Contents

Protein chains

275 a.a.

100 a.a.

Ligands

ALA-ALA-ALA-LYS-LYS-GLY-TYR-CYS-LEU

Waters ×274

PDB id:

6p2f

Name:

Immune system

Title:

Structure of a nested set of n-terminally extended mhc i-peptides provides novel insights into antigen processing and presentation

Structure:

Hla class i histocompatibility antigen, b-8 alpha chain. Chain: a. Fragment: unp residues 25-300. Synonym: mhc class i antigen b 8. Engineered: yes. Mutation: yes. Beta-2-microglobulin. Chain: b. Fragment: unp residues 21-119.

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: hla-b, hlab. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Gene: b2m, cdabp0092, hdcma22p. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

1.48Å R-factor: 0.216 R-free: 0.245

Authors:

L.Li,M.Batliwala,M.Bouvier

Key ref:

L.Li et al. (2019). ERAP1 enzyme-mediated trimming and structural analyses of MHC I-bound precursor peptides yield novel insights into antigen processing and presentation. J Biol Chem, 294, 18534-18544. PubMed id: 31601650 DOI: 10.1074/jbc.RA119.010102

Date:

21-May-19 Release date: 16-Oct-19

Protein chain

P01889  (1B07_HUMAN) -  HLA class I histocompatibility antigen, B alpha chain from Homo sapiens

Seq: 362 a.a.

Struc: 275 a.a.*

Protein chain

P61769  (B2MG_HUMAN) -  Beta-2-microglobulin from Homo sapiens

Seq: 119 a.a.

Struc: 100 a.a.*

* PDB and UniProt seqs differ at 14 residue positions (black crosses)

DOI no: 10.1074/jbc.RA119.010102

J Biol Chem 294:18534-18544 (2019)

PubMed id: 31601650

ERAP1 enzyme-mediated trimming and structural analyses of MHC I-bound precursor peptides yield novel insights into antigen processing and presentation.

L.Li, M.Batliwala, M.Bouvier.

ABSTRACT

Endoplasmic reticulum aminopeptidase 1 (ERAP1) and ERAP2 critically shape the major histocompatibility complex I (MHC I) immunopeptidome. The ERAPs remove N-terminal residues from antigenic precursor peptides and generate optimal-length peptides (i.e. 8-10-mers) to fit into the MHC class I groove. It is therefore intriguing that MHC class I molecules can present N-terminally extended peptides on the cell surface that can elicit CD8+ T-cell responses. This observation likely reflects gaps in our understanding of how antigens are processed by the ERAP enzymes. To better understand ERAPs' function in antigen processing, here we generated a nested set of N-terminally extended 10-20-mer peptides (RA)