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Plasminogen activation PDB id
1kdu
Jmol
Contents
Protein chain
85 a.a. *
* Residue conservation analysis
PDB id:
1kdu
Name: Plasminogen activation
Title: Sequential 1h nmr assignments and secondary structure of the kringle domain from urokinase
Structure: Plasminogen activator. Chain: a. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606
NMR struc: 1 models
Authors: X.Li,A.M.Bokman,M.Llinas,R.A.G.Smith,C.M.Dobson
Key ref:
X.Li et al. (1992). Sequential 1H NMR assignments and secondary structure of the kringle domain from urokinase. Biochemistry, 31, 9562-9571. PubMed id: 1327118 DOI: 10.1021/bi00155a008
Date:
15-Jul-93     Release date:   31-Oct-93    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P00749  (UROK_HUMAN) -  Urokinase-type plasminogen activator
Seq:
Struc: 		431 a.a.
85 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.4.21.73  - U-plasminogen activator.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Specific cleavage of Arg-|-Val bond in plasminogen to form plasmin.

 

 
DOI no: 10.1021/bi00155a008 Biochemistry 31:9562-9571 (1992)
PubMed id: 1327118  
 
 
Sequential 1H NMR assignments and secondary structure of the kringle domain from urokinase.
X.Li, R.A.Smith, C.M.Dobson.
 
  ABSTRACT  
 
The sequence-specific 1H NMR assignments of the 89-residue recombinant kringle domain from human urokinase are presented. These were achieved primarily by utilizing TOCSY and NOESY spectra in conjunction with COSY spectra recorded at 500 MHz and 600 MHz. Regular secondary structure elements have been derived from a qualitative interpretation of nuclear Overhauser enhancement, JNH alpha coupling constant, and amide proton exchange data. Two helices have been identified. One helix, involving Ser40-Gly46, corresponds to that reported for t-PA kringle 2 (Byeon et al., 1991), but does not exist in other kringles with known structures. The second helix, in the region Asn26-Gln33, is thus far unique to the urokinase kringle. Three antiparallel beta-sheets and three tight turns have also been identified, which correspond exactly to those identified in t-PA kringle 2 both in solution and in the crystalline state (de Vos et al., 1992). Despite the very different ligand binding properties of the urokinase kringle, NOE data indicate that the tertiary fold of the molecule conforms closely to that found for other kringles.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
14717962 J.H.Geiger, and S.E.Cnudde (2004).
What the structure of angiostatin may tell us about its mechanism of action.
  J Thromb Haemost, 2, 23-34.  
  8069221 K.Padmanabhan, T.P.Wu, K.G.Ravichandran, and A.Tulinsky (1994).
Kringle-kringle interactions in multimer kringle structures.
  Protein Sci, 3, 898-910.
PDB codes: 1pmk 1pml
8181475 M.R.Rejante, and M.Llinás (1994).
1H-NMR assignments and secondary structure of human plasminogen kringle 1.
  Eur J Biochem, 221, 927-937.  
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