PDBsum entry 4duu

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protein links
Hydrolase PDB id
Protein chain
682 a.a.
Waters ×35
PDB id:
Name: Hydrolase
Title: The x-ray crystal structure of full-length type i human plas
Structure: Plasminogen. Chain: a. Synonym: serine protease. Ec:
Source: Homo sapiens. Human. Organism_taxid: 9606. Tissue: plasma
5.20Å     R-factor:   0.270     R-free:   0.312
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
22-Feb-12     Release date:   28-Mar-12    
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Protein chain
Pfam   ArchSchema ?
P00747  (PLMN_HUMAN) -  Plasminogen
810 a.a.
682 a.a.
Key:    PfamA domain  Secondary structure

 Enzyme reactions 
   Enzyme class: E.C.  - 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   23 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.
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.