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PDBsum entry 4dur

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protein ligands metals Protein-protein interface(s) links
Hydrolase PDB id
4dur
Jmol
Contents
Protein chain
756 a.a.
Ligands
BCT ×2
ACT
NAG-GAL-SIA ×2
Metals
_CL ×7
__K ×2
Waters ×1436
PDB id:
4dur
Name: Hydrolase
Title: The x-ray crystal structure of full-length type ii human pla
Structure: Plasminogen. Chain: a, b. Synonym: serine protease. Ec: 3.4.21.7
Source: Homo sapiens. Human. Organism_taxid: 9606. Tissue: plasma
Resolution:
2.45Å     R-factor:   0.191     R-free:   0.215
Authors: R.H.P.Law,T.Caradoc-Davies,J.C.Whisstock
Key ref: R.H.Law et al. (2012). The X-ray crystal structure of full-length human plasminogen. Cell Rep, 1, 185-190. PubMed id: 22832192 DOI: 10.1016/j.celrep.2012.02.012
Date:
22-Feb-12     Release date:   28-Mar-12    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P00747  (PLMN_HUMAN) -  Plasminogen
Seq:
Struc:
 
Seq:
Struc:
810 a.a.
756 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.4.21.7  - Plasmin.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Preferential cleavage: Lys-|-Xaa > Arg-|-Xaa; higher selectivity than trypsin. Converts fibrin into soluble products.
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   10 terms 
  Biological process     mononuclear cell migration   22 terms 
  Biochemical function     catalytic activity     10 terms  

 

 
DOI no: 10.1016/j.celrep.2012.02.012 Cell Rep 1:185-190 (2012)
PubMed id: 22832192  
 
 
The X-ray crystal structure of full-length human plasminogen.
R.H.Law, T.Caradoc-Davies, N.Cowieson, A.J.Horvath, A.J.Quek, J.A.Encarnacao, D.Steer, A.Cowan, Q.Zhang, B.G.Lu, R.N.Pike, A.I.Smith, P.B.Coughlin, J.C.Whisstock.
 
  ABSTRACT  
 
Plasminogen is the proenzyme precursor of the primary fibrinolytic protease plasmin. Circulating plasminogen, which comprises a Pan-apple (PAp) domain, five kringle domains (KR1-5), and a serine protease (SP) domain, adopts a closed, activation-resistant conformation. The kringle domains mediate interactions with fibrin clots and cell-surface receptors. These interactions trigger plasminogen to adopt an open form that can be cleaved and converted to plasmin by tissue-type and urokinase-type plasminogen activators. Here, the structure of closed plasminogen reveals that the PAp and SP domains, together with chloride ions, maintain the closed conformation through interactions with the kringle array. Differences in glycosylation alter the position of KR3, although in all structures the loop cleaved by plasminogen activators is inaccessible. The ligand-binding site of KR1 is exposed and likely governs proenzyme recruitment to targets. Furthermore, analysis of our structure suggests that KR5 peeling away from the PAp domain may initiate plasminogen conformational change.