3SE6: Crystal structure of the human Endoplasmic Reticulum Aminopeptidase 2

Citation:
Abstract
Endoplasmic reticulum aminopeptidases ERAP1 and ERAP2 cooperate to trim a vast variety of antigenic peptide precursors to generate mature epitopes for binding to major histocompatibility class I molecules. We report here the first structure of ERAP2 determined at 3.08 A by X-ray crystallography. On the basis of residual electron density, a lysine residue has been modeled in the active site of the enzyme; thus, the structure corresponds to an enzyme-product complex. The overall domain organization is highly similar to that of the recently determined structure of ERAP1 in its closed conformation. A large internal cavity adjacent to the catalytic site can accommodate large peptide substrates. The ERAP2 structure provides a structural explanation for the different peptide N-terminal specificities between ERAP1 and ERAP2 and suggests that such differences extend throughout the whole peptide sequence. A noncrystallographic dimer observed may constitute a model for a proposed ERAP1-ERAP2 heterodimer. Overall, the structure helps explain how two homologous aminopeptidases cooperate to process a large variety of sequences, a key property of their biological role.
PDB ID: 3SE6Download
MMDB ID: 95902
PDB Deposition Date: 2011/6/10
Updated in MMDB: 2011/12
Experimental Method:
x-ray diffraction
Resolution: 3.08  Å
Source Organism:
Similar Structures:
Biological Unit for 3SE6: monomeric; determined by author and by software (PISA)
Molecular Components in 3SE6
Label Count Molecule
Protein (1 molecule)
1
Endoplasmic Reticulum Aminopeptidase 2(Gene symbol: ERAP2)
Molecule annotation
Chemicals (13 molecules)
1
1
2
1
3
8
4
1
5
2
* Click molecule labels to explore molecular sequence information.

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