1TPG

F1-G MODULE PAIR RESIDUES 1-91 (C83S) OF TISSUE-TYPE PLASMINOGEN ACTIVATOR (T-PA) (NMR, 298K, PH2.95, REPRESENTATIVE STRUCTURE)


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Submitted: 

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This is version 1.3 of the entry. See complete history


Literature

The solution structure and backbone dynamics of the fibronectin type I and epidermal growth factor-like pair of modules of tissue-type plasminogen activator.

Smith, B.O.Downing, A.K.Driscoll, P.C.Dudgeon, T.J.Campbell, I.D.

(1995) Structure 3: 823-833

  • DOI: https://doi.org/10.1016/s0969-2126(01)00217-9
  • Primary Citation of Related Structures:  
    1TPG

  • PubMed Abstract: 

    The thrombolytic serine protease tissue-type plasminogen activator (t-PA) is a classical modular protein consisting of three types of domain in addition to the serine protease domain: F1 (homologous to fibronectin type I); G (epidermal growth factor-like) and kringle. Biochemical data suggest that the F1 and G modules play a major role in the binding of t-PA to fibrin and to receptors on hepatocytes.


  • Organizational Affiliation

    Oxford Centre for Molecular Sciences, UK.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
T-PLASMINOGEN ACTIVATOR F1-G91Homo sapiensMutation(s): 0 
EC: 3.4.21.68
UniProt & NIH Common Fund Data Resources
Find proteins for P00750 (Homo sapiens)
Explore P00750 
Go to UniProtKB:  P00750
PHAROS:  P00750
GTEx:  ENSG00000104368 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP00750
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Submitted: 

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1995-09-15
    Type: Initial release
  • Version 1.1: 2008-03-24
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2022-03-02
    Changes: Database references, Derived calculations, Other