Plasmepsin

Function

Plasmepsin (Plm) is a hemoglobin-degrading enzyme produced by the plasmodium parasite. It is an aspartic acid protease having 2 aspartic acid residues in the active site. Ten Plm isoforms are known which are named Plm I, II, etc and Histo-Aspartic Protease (HAP).

• Proplasmepsin II exhibits a large shift between its domains which renders the protease inactive.

Relevance

Plm is a potential target for anti-malaria drugs.

3D structures of plasmepsin

Updated on 04-July-2016

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• Histo-Aspartic Protease
  • 3fns, 3qvc – PfHAP - Plasmodium falciparum
    
  • 3fnt – PfHAP + pepstatin
    
  • 3fnu, 3qvi – PfHAP + inhibitor
    
• Plasmepsin I
  • 3qrv – PfPlm I residues 117-457
    
  • 3qs1 - PfPlm I residues 117-457 + inhibitor
• Plasmepsin II
  • 1lf4 – PfPlm II
    
  • 3f9q – PfPlm II (mutant)
    
  • 2r9b – PfPlm II + peptide inhibitor
    
  • 1w6h, 2bju, 1lf2, 1lf3, 1lee, 2igx, 2igy, 4cku – PfPlm II + inhibitor
    
  • 1w6i, 1xdh, 1xe5, 1xe6, 1me6, 1sme – PfPlm II + pepstatin derivative
    
  • 1m43 - PfPlm II (mutant) + pepstatin derivative
    
• Plasmepsin IV
  • 2anl – Plm IV + statine derivative – Plasmodium malariae
    
  • 1ls5 - PfPlm IV + pepstatin derivative
    
• Proplasmepsin II
  • 1pfz - PfProPlm II
    
  • 1miq – PvProPlm II – Plasmodium vivax
    
  • 1qs8 - PvPlm + pepstatin derivative
    

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Alexander Berchansky, Michal Harel, Joel L. Sussman, Jaime Prilusky