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PDBsum entry 1ygu
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Contents |
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* Residue conservation analysis
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PDB id:
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Hydrolase
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Title:
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Crystal structure of the tandem phosphatase domains of rptp cd45 with a ptyr peptide
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Structure:
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Leukocyte common antigen. Chain: a, b. Fragment: d1 and d2 ptp domains. Synonym: l-ca, cd45 antigen, t200. Engineered: yes. Mutation: yes. Polyoma middle t antigen. Chain: c, d. Fragment: middle t antigen (residues 248-251, sws:p03077).
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: ptprc, cd45. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693. Synthetic: yes. Other_details: polyoma middle t antigen ptyr peptide
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Biol. unit:
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Dimer (from
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Resolution:
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2.90Å
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R-factor:
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0.262
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R-free:
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0.305
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Authors:
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H.Nam,F.Poy,H.Saito,C.A.Frederick
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Key ref:
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H.J.Nam
et al.
(2005).
Structural basis for the function and regulation of the receptor protein tyrosine phosphatase CD45.
J Exp Med,
201,
441-452.
PubMed id:
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Date:
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05-Jan-05
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Release date:
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22-Feb-05
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PROCHECK
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Headers
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References
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P08575
(PTPRC_HUMAN) -
Receptor-type tyrosine-protein phosphatase C from Homo sapiens
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Seq:
Struc:
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1306 a.a.
571 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 3 residue positions (black
crosses)
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Enzyme class:
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E.C.3.1.3.48
- protein-tyrosine-phosphatase.
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Reaction:
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O-phospho-L-tyrosyl-[protein] + H2O = L-tyrosyl-[protein] + phosphate
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O-phospho-L-tyrosyl-[protein]
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+
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H2O
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=
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L-tyrosyl-[protein]
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+
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phosphate
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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J Exp Med
201:441-452
(2005)
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PubMed id:
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Structural basis for the function and regulation of the receptor protein tyrosine phosphatase CD45.
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H.J.Nam,
F.Poy,
H.Saito,
C.A.Frederick.
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ABSTRACT
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CD45 is the prototypic member of transmembrane receptor-like protein tyrosine
phosphatases (RPTPs) and has essential roles in immune functions. The
cytoplasmic region of CD45, like many other RPTPs, contains two homologous
protein tyrosine phosphatase domains, active domain 1 (D1) and catalytically
impaired domain 2 (D2). Here, we report crystal structure of the cytoplasmic
D1D2 segment of human CD45 in native and phosphotyrosyl peptide-bound forms. The
tertiary structures of D1 and D2 are very similar, but doubly phosphorylated
CD3zeta immunoreceptor tyrosine-based activation motif peptide binds only the D1
active site. The D2 "active site" deviates from the other active sites
significantly to the extent that excludes any possibility of catalytic activity.
The relative orientation of D1 and D2 is very similar to that observed in
leukocyte common antigen-related protein with both active sites in an open
conformation and is restrained through an extensive network of hydrophobic
interactions, hydrogen bonds, and salt bridges. This crystal structure is
incompatible with the wedge model previously suggested for CD45 regulation.
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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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C.W.Cairo,
R.Das,
A.Albohy,
Q.J.Baca,
D.Pradhan,
J.S.Morrow,
D.Coombs,
and
D.E.Golan
(2010).
Dynamic regulation of CD45 lateral mobility by the spectrin-ankyrin cytoskeleton of T cells.
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J Biol Chem,
285,
11392-11401.
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A.E.Hower,
P.J.Beltran,
and
J.L.Bixby
(2009).
Dimerization of tyrosine phosphatase PTPRO decreases its activity and ability to inactivate TrkC.
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J Neurochem,
110,
1635-1647.
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A.J.Barr,
E.Ugochukwu,
W.H.Lee,
O.N.King,
P.Filippakopoulos,
I.Alfano,
P.Savitsky,
N.A.Burgess-Brown,
S.Müller,
and
S.Knapp
(2009).
Large-scale structural analysis of the classical human protein tyrosine phosphatome.
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Cell,
136,
352-363.
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PDB codes:
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M.L.Hermiston,
J.Zikherman,
A.L.Tan,
V.C.Lam,
N.M.Cresalia,
N.Oksenberg,
N.Goren,
D.Brassat,
J.R.Oksenberg,
and
A.Weiss
(2009).
Differential impact of the CD45 juxtamembrane wedge on central and peripheral T cell receptor responses.
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Proc Natl Acad Sci U S A,
106,
546-551.
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M.L.Hermiston,
J.Zikherman,
and
J.W.Zhu
(2009).
CD45, CD148, and Lyp/Pep: critical phosphatases regulating Src family kinase signaling networks in immune cells.
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Immunol Rev,
228,
288-311.
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S.H.Lim,
S.K.Kwon,
M.K.Lee,
J.Moon,
D.G.Jeong,
E.Park,
S.J.Kim,
B.C.Park,
S.C.Lee,
S.E.Ryu,
D.Y.Yu,
B.H.Chung,
E.Kim,
P.K.Myung,
and
J.R.Lee
(2009).
Synapse formation regulated by protein tyrosine phosphatase receptor T through interaction with cell adhesion molecules and Fyn.
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EMBO J,
28,
3564-3578.
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A.Groen,
J.Overvoorde,
T.van der Wijk,
and
J.den Hertog
(2008).
Redox regulation of dimerization of the receptor protein-tyrosine phosphatases RPTPalpha, LAR, RPTPmu and CD45.
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FEBS J,
275,
2597-2604.
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H.P.Monteiro,
R.J.Arai,
and
L.R.Travassos
(2008).
Protein tyrosine phosphorylation and protein tyrosine nitration in redox signaling.
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Antioxid Redox Signal,
10,
843-889.
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J.den Hertog,
A.Ostman,
and
F.D.Böhmer
(2008).
Protein tyrosine phosphatases: regulatory mechanisms.
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FEBS J,
275,
831-847.
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L.Tabernero,
A.R.Aricescu,
E.Y.Jones,
and
S.E.Szedlacsek
(2008).
Protein tyrosine phosphatases: structure-function relationships.
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FEBS J,
275,
867-882.
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R.J.Salmond,
L.McNeill,
N.Holmes,
and
D.R.Alexander
(2008).
CD4+ T cell hyper-responsiveness in CD45 transgenic mice is independent of isoform.
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Int Immunol,
20,
819-827.
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S.Kirchberger,
O.Majdic,
S.Blüml,
C.Schrauf,
J.Leitner,
C.Gerner,
W.Paster,
N.Gundacker,
M.Sibilia,
and
J.Stöckl
(2008).
The cytoplasmic tail of CD45 is released from activated phagocytes and can act as an inhibitory messenger for T cells.
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Blood,
112,
1240-1248.
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T.Vang,
A.V.Miletic,
Y.Arimura,
L.Tautz,
R.C.Rickert,
and
T.Mustelin
(2008).
Protein tyrosine phosphatases in autoimmunity.
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Annu Rev Immunol,
26,
29-55.
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A.R.Aricescu,
and
E.Y.Jones
(2007).
Immunoglobulin superfamily cell adhesion molecules: zippers and signals.
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Curr Opin Cell Biol,
19,
543-550.
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S.C.Almo,
J.B.Bonanno,
J.M.Sauder,
S.Emtage,
T.P.Dilorenzo,
V.Malashkevich,
S.R.Wasserman,
S.Swaminathan,
S.Eswaramoorthy,
R.Agarwal,
D.Kumaran,
M.Madegowda,
S.Ragumani,
Y.Patskovsky,
J.Alvarado,
U.A.Ramagopal,
J.Faber-Barata,
M.R.Chance,
A.Sali,
A.Fiser,
Z.Y.Zhang,
D.S.Lawrence,
and
S.K.Burley
(2007).
Structural genomics of protein phosphatases.
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J Struct Funct Genomics,
8,
121-140.
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PDB codes:
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S.Lee,
C.Faux,
J.Nixon,
D.Alete,
J.Chilton,
M.Hawadle,
and
A.W.Stoker
(2007).
Dimerization of protein tyrosine phosphatase sigma governs both ligand binding and isoform specificity.
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Mol Cell Biol,
27,
1795-1808.
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A.J.Barr,
J.E.Debreczeni,
J.Eswaran,
and
S.Knapp
(2006).
Crystal structure of human protein tyrosine phosphatase 14 (PTPN14) at 1.65-A resolution.
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Proteins,
63,
1132-1136.
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PDB code:
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A.Ostman,
C.Hellberg,
and
F.D.Böhmer
(2006).
Protein-tyrosine phosphatases and cancer.
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Nat Rev Cancer,
6,
307-320.
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E.Z.Tchilian,
and
P.C.Beverley
(2006).
Altered CD45 expression and disease.
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Trends Immunol,
27,
146-153.
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J.Eswaran,
J.E.Debreczeni,
E.Longman,
A.J.Barr,
and
S.Knapp
(2006).
The crystal structure of human receptor protein tyrosine phosphatase kappa phosphatase domain 1.
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Protein Sci,
15,
1500-1505.
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PDB codes:
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N.Holmes
(2006).
CD45: all is not yet crystal clear.
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Immunology,
117,
145-155.
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N.K.Tonks
(2006).
Protein tyrosine phosphatases: from genes, to function, to disease.
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Nat Rev Mol Cell Biol,
7,
833-846.
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R.Dawes,
S.Petrova,
Z.Liu,
D.Wraith,
P.C.Beverley,
and
E.Z.Tchilian
(2006).
Combinations of CD45 isoforms are crucial for immune function and disease.
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J Immunol,
176,
3417-3425.
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S.J.van Vliet,
S.I.Gringhuis,
T.B.Geijtenbeek,
and
Y.van Kooyk
(2006).
Regulation of effector T cells by antigen-presenting cells via interaction of the C-type lectin MGL with CD45.
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Nat Immunol,
7,
1200-1208.
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M.L.Hermiston,
A.L.Tan,
V.A.Gupta,
R.Majeti,
and
A.Weiss
(2005).
The juxtamembrane wedge negatively regulates CD45 function in B cells.
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Immunity,
23,
635-647.
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T.Uinuk-Ool,
N.Nikolaidis,
A.Sato,
W.E.Mayer,
and
J.Klein
(2005).
Organization, alternative splicing, polymorphism, and phylogenetic position of lamprey CD45 gene.
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Immunogenetics,
57,
607-617.
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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
