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* Residue conservation analysis
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PDB id:
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Immune system/isomerase
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Title:
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Tapasin/erp57 heterodimer
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Structure:
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Protein disulfide-isomerase a3erp57. Chain: a, c. Synonym: erp57, disulfide isomerase er-60, erp60, 58 kda microsomal protein, p58, erp57, 58 kda glucose-regulated protein. Engineered: yes. Mutation: yes. Other_details: covalently linked to tapasin via sulfide bond. Tapasin. Chain: b, d.
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: pdia3, erp57, erp60, grp58. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108. Gene: tapbp, ngs17, tapa.
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Resolution:
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2.60Å
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R-factor:
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0.245
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R-free:
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0.285
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Authors:
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G.Dong,K.M.Reinisch
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Key ref:
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G.Dong
et al.
(2009).
Insights into MHC class I peptide loading from the structure of the tapasin-ERp57 thiol oxidoreductase heterodimer.
Immunity,
30,
21-32.
PubMed id:
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Date:
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13-Nov-08
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Release date:
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13-Jan-09
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PROCHECK
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Headers
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References
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Enzyme class:
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Chains A, C:
E.C.5.3.4.1
- protein disulfide-isomerase.
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Reaction:
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Rearrangement of both intrachain and interchain disulfide bonds in proteins to form the native structures.
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Immunity
30:21-32
(2009)
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PubMed id:
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Insights into MHC class I peptide loading from the structure of the tapasin-ERp57 thiol oxidoreductase heterodimer.
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G.Dong,
P.A.Wearsch,
D.R.Peaper,
P.Cresswell,
K.M.Reinisch.
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ABSTRACT
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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.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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D.Horst,
M.E.Ressing,
and
E.J.Wiertz
(2011).
Exploiting human herpesvirus immune evasion for therapeutic gain: potential and pitfalls.
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Immunol Cell Biol,
89,
359-366.
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J.Riemer,
H.G.Hansen,
C.Appenzeller-Herzog,
L.Johansson,
and
L.Ellgaard
(2011).
Identification of the PDI-Family Member ERp90 as an Interaction Partner of ERFAD.
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PLoS One,
6,
e17037.
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L.A.Rutkevich,
and
D.B.Williams
(2011).
Participation of lectin chaperones and thiol oxidoreductases in protein folding within the endoplasmic reticulum.
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Curr Opin Cell Biol,
23,
157-166.
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P.A.Wearsch,
D.R.Peaper,
and
P.Cresswell
(2011).
Essential glycan-dependent interactions optimize MHC class I peptide loading.
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Proc Natl Acad Sci U S A,
108,
4950-4955.
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A.Van Hateren,
E.James,
A.Bailey,
A.Phillips,
N.Dalchau,
and
T.Elliott
(2010).
The cell biology of major histocompatibility complex class I assembly: towards a molecular understanding.
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Tissue Antigens,
76,
259-275.
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D.Parcej,
and
R.Tampé
(2010).
ABC proteins in antigen translocation and viral inhibition.
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Nat Chem Biol,
6,
572-580.
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E.Pedone,
D.Limauro,
K.D'Ambrosio,
G.De Simone,
and
S.Bartolucci
(2010).
Multiple catalytically active thioredoxin folds: a winning strategy for many functions.
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Cell Mol Life Sci,
67,
3797-3814.
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G.Kozlov,
P.Määttänen,
D.Y.Thomas,
and
K.Gehring
(2010).
A structural overview of the PDI family of proteins.
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FEBS J,
277,
3924-3936.
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H.Fabian,
H.Huser,
B.Loll,
A.Ziegler,
D.Naumann,
and
B.Uchanska-Ziegler
(2010).
HLA-B27 heavy chains distinguished by a micropolymorphism exhibit differential flexibility.
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Arthritis Rheum,
62,
978-987.
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K.Inaba,
S.Masui,
H.Iida,
S.Vavassori,
R.Sitia,
and
M.Suzuki
(2010).
Crystal structures of human Ero1α reveal the mechanisms of regulated and targeted oxidation of PDI.
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EMBO J,
29,
3330-3343.
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PDB codes:
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L.C.Simone,
X.Wang,
A.Tuli,
and
J.C.Solheim
(2010).
Effect of a tapasin mutant on the assembly of the mouse MHC class I molecule H2-K(d).
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Immunol Cell Biol,
88,
57-62.
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L.E.Kropp,
M.Garg,
and
R.J.Binder
(2010).
Ovalbumin-derived precursor peptides are transferred sequentially from gp96 and calreticulin to MHC class I in the endoplasmic reticulum.
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J Immunol,
184,
5619-5627.
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N.Del Cid,
E.Jeffery,
S.M.Rizvi,
E.Stamper,
L.R.Peters,
W.C.Brown,
C.Provoda,
and
M.Raghavan
(2010).
Modes of calreticulin recruitment to the major histocompatibility complex class I assembly pathway.
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J Biol Chem,
285,
4520-4535.
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P.V.Praveen,
R.Yaneva,
H.Kalbacher,
and
S.Springer
(2010).
Tapasin edits peptides on MHC class I molecules by accelerating peptide exchange.
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Eur J Immunol,
40,
214-224.
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R.A.Colbert,
M.L.DeLay,
E.I.Klenk,
and
G.Layh-Schmitt
(2010).
From HLA-B27 to spondyloarthritis: a journey through the ER.
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Immunol Rev,
233,
181-202.
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S.M.Rizvi,
and
M.Raghavan
(2010).
Mechanisms of function of tapasin, a critical major histocompatibility complex class I assembly factor.
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Traffic,
11,
332-347.
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A.K.Wallis,
A.Sidhu,
L.J.Byrne,
M.J.Howard,
L.W.Ruddock,
R.A.Williamson,
and
R.B.Freedman
(2009).
The ligand-binding b' domain of human protein disulphide-isomerase mediates homodimerization.
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Protein Sci,
18,
2569-2577.
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C.Schölz,
and
R.Tampé
(2009).
The peptide-loading complex--antigen translocation and MHC class I loading.
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Biol Chem,
390,
783-794.
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D.Hatherley,
S.C.Graham,
K.Harlos,
D.I.Stuart,
and
A.N.Barclay
(2009).
Structure of signal-regulatory protein alpha: a link to antigen receptor evolution.
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J Biol Chem,
284,
26613-26619.
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PDB code:
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E.Procko,
and
R.Gaudet
(2009).
Antigen processing and presentation: TAPping into ABC transporters.
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Curr Opin Immunol,
21,
84-91.
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F.Hatahet,
and
L.W.Ruddock
(2009).
Protein disulfide isomerase: a critical evaluation of its function in disulfide bond formation.
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Antioxid Redox Signal,
11,
2807-2850.
|
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G.Kozlov,
P.Määttänen,
J.D.Schrag,
G.L.Hura,
L.Gabrielli,
M.Cygler,
D.Y.Thomas,
and
K.Gehring
(2009).
Structure of the noncatalytic domains and global fold of the protein disulfide isomerase ERp72.
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Structure,
17,
651-659.
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PDB code:
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J.G.Donaldson,
and
D.B.Williams
(2009).
Intracellular assembly and trafficking of MHC class I molecules.
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Traffic,
10,
1745-1752.
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L.C.Simone,
X.Wang,
and
J.C.Solheim
(2009).
A transmembrane tail: interaction of tapasin with TAP and the MHC class I molecule.
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Mol Immunol,
46,
2147-2150.
|
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N.Vigneron,
D.R.Peaper,
R.M.Leonhardt,
and
P.Cresswell
(2009).
Functional significance of tapasin membrane association and disulfide linkage to ERp57 in MHC class I presentation.
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Eur J Immunol,
39,
2371-2376.
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R.Abele,
and
R.Tampé
(2009).
Peptide trafficking and translocation across membranes in cellular signaling and self-defense strategies.
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Curr Opin Cell Biol,
21,
508-515.
|
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|
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T.Elliott
(2009).
More images that yet fresh images Beget.
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Immunity,
30,
1-2.
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T.H.Hansen,
and
M.Bouvier
(2009).
MHC class I antigen presentation: learning from viral evasion strategies.
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Nat Rev Immunol,
9,
503-513.
|
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|
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Y.Zhang,
G.Kozlov,
C.L.Pocanschi,
U.Brockmeier,
B.S.Ireland,
P.Maattanen,
C.Howe,
T.Elliott,
K.Gehring,
and
D.B.Williams
(2009).
ERp57 does not require interactions with calnexin and calreticulin to promote assembly of class I histocompatibility molecules, and it enhances peptide loading independently of its redox activity.
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J Biol Chem,
284,
10160-10173.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
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Links
