Structural highlights
3f8u is a 4 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
|
| Ligands: | |
| Gene: | PDIA3, ERP57, ERP60, GRP58 (HUMAN), TAPBP, NGS17, TAPA (HUMAN) |
| Activity: | Protein disulfide-isomerase, with EC number 5.3.4.1 |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[TPSN_HUMAN] Involved in the association of MHC class I with transporter associated with antigen processing (TAP) and in the assembly of MHC class I with peptide (peptide loading).[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Tapasin is a glycoprotein critical for loading major histocompatibility complex (MHC) class I molecules with high-affinity peptides. It functions within the multimeric peptide-loading complex (PLC) as a disulfide-linked, stable heterodimer with the thiol oxidoreductase ERp57, and this covalent interaction is required to support optimal PLC activity. Here, we present the 2.6 A resolution structure of the tapasin-ERp57 core of the PLC. The structure revealed that tapasin interacts with both ERp57 catalytic domains, accounting for the stability of the heterodimer, and provided an example of a protein disulfide isomerase family member interacting with substrate. Mutational analysis identified a conserved surface on tapasin that interacted with MHC class I molecules and was critical for peptide loading and editing functions of the tapasin-ERp57 heterodimer. By combining the tapasin-ERp57 structure with those of other defined PLC components, we present a molecular model that illuminates the processes involved in MHC class I peptide loading.
Insights into MHC Class I Peptide Loading from the Structure of the Tapasin-ERp57 Thiol Oxidoreductase Heterodimer.,Dong G, Wearsch PA, Peaper DR, Cresswell P, Reinisch KM Immunity. 2008 Dec 30. PMID:19119025[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Li S, Paulsson KM, Chen S, Sjogren HO, Wang P. Tapasin is required for efficient peptide binding to transporter associated with antigen processing. J Biol Chem. 2000 Jan 21;275(3):1581-6. PMID:10636848
- ↑ Dong G, Wearsch PA, Peaper DR, Cresswell P, Reinisch KM. Insights into MHC Class I Peptide Loading from the Structure of the Tapasin-ERp57 Thiol Oxidoreductase Heterodimer. Immunity. 2008 Dec 30. PMID:19119025 doi:S1074-7613(08)00544-X
