PDBsum entry 2a3k

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protein ligands links
Signaling protein PDB id
Protein chain
272 a.a. *
PO4 ×4
Waters ×32
* Residue conservation analysis
PDB id:
Name: Signaling protein
Title: Crystal structure of the human protein tyrosine phosphatase, (heptp, hematopoietic protein tyrosine phosphatase)
Structure: Protein tyrosine phosphatase, non-receptor type 7 1. Chain: a. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: ptpn7. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
2.55Å     R-factor:   0.222     R-free:   0.275
Authors: A.Barr,A.P.Turnbull,S.Das,J.Eswaran,J.E.Debreczeni,E.Longman N.Burgess,O.Gileadi,M.Sundstrom,C.Arrowsmith,A.Edwards,F.Vo S.Knapp,Structural Genomics Consortium (Sgc)
Key ref:
J.Eswaran et al. (2006). The crystal structure of human receptor protein tyrosine phosphatase kappa phosphatase domain 1. Protein Sci, 15, 1500-1505. PubMed id: 16672235 DOI: 10.1110/ps.062128706
24-Jun-05     Release date:   19-Jul-05    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
P35236  (PTN7_HUMAN) -  Tyrosine-protein phosphatase non-receptor type 7
360 a.a.
272 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.  - Protein-tyrosine-phosphatase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Protein tyrosine phosphate + H2O = protein tyrosine + phosphate
Protein tyrosine phosphate
+ H(2)O
= protein tyrosine
Bound ligand (Het Group name = PO4)
corresponds exactly
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     dephosphorylation   2 terms 
  Biochemical function     phosphatase activity     2 terms  


DOI no: 10.1110/ps.062128706 Protein Sci 15:1500-1505 (2006)
PubMed id: 16672235  
The crystal structure of human receptor protein tyrosine phosphatase kappa phosphatase domain 1.
J.Eswaran, J.E.Debreczeni, E.Longman, A.J.Barr, S.Knapp.
The receptor-type protein tyrosine phosphatases (RPTPs) are integral membrane proteins composed of extracellular adhesion molecule-like domains, a single transmembrane domain, and a cytoplasmic domain. The cytoplasmic domain consists of tandem PTP domains, of which the D1 domain is enzymatically active. RPTPkappa is a member of the R2A/IIb subfamily of RPTPs along with RPTPmu, RPTPrho, and RPTPlambda. Here, we have determined the crystal structure of catalytically active, monomeric D1 domain of RPTPkappa at 1.9 A. Structural comparison with other PTP family members indicates an overall classical PTP architecture of twisted mixed beta-sheets flanked by alpha-helices, in which the catalytically important WPD loop is in an unhindered open conformation. Though the residues forming the dimeric interface in the RPTPmu structure are all conserved, they are not involved in the protein-protein interaction in RPTPkappa. The N-terminal beta-strand, formed by betax association with betay, is conserved only in RPTPs but not in cytosolic PTPs, and this feature is conserved in the RPTPkappa structure forming a beta-strand. Analytical ultracentrifugation studies show that the presence of reducing agents and higher ionic strength are necessary to maintain RPTPkappa as a monomer. In this family the crystal structure of catalytically active RPTPmu D1 was solved as a dimer, but the dimerization was proposed to be a consequence of crystallization since the protein was monomeric in solution. In agreement, we show that RPTPkappa is monomeric in solution and crystal structure.
  Selected figure(s)  
Figure 2.
Figure 2. Three-dimensional structure of RPTP . (Red) -Helices; (green) -strands; (magenta) 3[10]-helices. The helix-turn-helix segment ( 1', 2') and the -strand formed by association of x and y are labeled. The corresponding conserved residues involved in dimerization of RPTPµ are shown in ball-and-stick representation.
  The above figure is reprinted by permission from the Protein Society: Protein Sci (2006, 15, 1500-1505) copyright 2006.  
  Figure was selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
19573017 A.E.Hower, P.J.Beltran, and J.L.Bixby (2009).
Dimerization of tyrosine phosphatase PTPRO decreases its activity and ability to inactivate TrkC.
  J Neurochem, 110, 1635-1647.  
19816407 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.
  EMBO J, 28, 3564-3578.  
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