2OOQ

Crystal Structure of the Human Receptor Phosphatase PTPRT


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.80 Å
  • R-Value Free: 0.188 
  • R-Value Work: 0.145 
  • R-Value Observed: 0.147 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history


Literature

Large-scale structural analysis of the classical human protein tyrosine phosphatome.

Barr, A.J.Ugochukwu, E.Lee, W.H.King, O.N.Filippakopoulos, P.Alfano, I.Savitsky, P.Burgess-Brown, N.A.Muller, S.Knapp, S.

(2009) Cell 136: 352-363

  • DOI: https://doi.org/10.1016/j.cell.2008.11.038
  • Primary Citation of Related Structures:  
    2AHS, 2B49, 2CFV, 2CJZ, 2GJT, 2H4V, 2I75, 2JJD, 2NLK, 2NZ6, 2OC3, 2OOQ, 2P6X, 2PA5, 2QEP, 3B7O

  • PubMed Abstract: 

    Protein tyrosine phosphatases (PTPs) play a critical role in regulating cellular functions by selectively dephosphorylating their substrates. Here we present 22 human PTP crystal structures that, together with prior structural knowledge, enable a comprehensive analysis of the classical PTP family. Despite their largely conserved fold, surface properties of PTPs are strikingly diverse. A potential secondary substrate-binding pocket is frequently found in phosphatases, and this has implications for both substrate recognition and development of selective inhibitors. Structural comparison identified four diverse catalytic loop (WPD) conformations and suggested a mechanism for loop closure. Enzymatic assays revealed vast differences in PTP catalytic activity and identified PTPD1, PTPD2, and HDPTP as catalytically inert protein phosphatases. We propose a "head-to-toe" dimerization model for RPTPgamma/zeta that is distinct from the "inhibitory wedge" model and that provides a molecular basis for inhibitory regulation. This phosphatome resource gives an expanded insight into intrafamily PTP diversity, catalytic activity, substrate recognition, and autoregulatory self-association.


  • Organizational Affiliation

    University of Oxford, Structural Genomics Consortium, Old Road Campus Research Building, Roosevelt Drive, Headington, Oxford, OX3 7DQ, UK. alastair.barr@sgc.ox.ac.uk


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Receptor-type tyrosine-protein phosphatase T
A, B
286Homo sapiensMutation(s): 0 
Gene Names: PTPRTKIAA0283
EC: 3.1.3.48
UniProt & NIH Common Fund Data Resources
Find proteins for O14522 (Homo sapiens)
Explore O14522 
Go to UniProtKB:  O14522
PHAROS:  O14522
GTEx:  ENSG00000196090 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupO14522
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.80 Å
  • R-Value Free: 0.188 
  • R-Value Work: 0.145 
  • R-Value Observed: 0.147 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 37.186α = 90
b = 86.697β = 99.89
c = 91.12γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
CrystalCleardata collection
MOSFLMdata reduction
CCP4data scaling
PHASERphasing

Structure Validation

View Full Validation Report



Entry History 

Revision History  (Full details and data files)

  • Version 1.0: 2007-02-20
    Type: Initial release
  • Version 1.1: 2008-05-01
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Advisory, Version format compliance
  • Version 1.3: 2018-04-04
    Changes: Data collection
  • Version 1.4: 2023-08-30
    Changes: Data collection, Database references, Derived calculations, Refinement description