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Literature summary for 3.4.25.2 extracted from

  • Subramaniam, S.; Mohmmed, A.; Gupta, D.
    Molecular modeling studies of the interaction between Plasmodium falciparum HslU and HslV subunits. (2009), J. Biomol. Struct. Dyn., 26, 473-479.
    View publication on PubMed

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Plasmodium falciparum the HslUV complex is an assembly of heat shock locus gene products U and V. The formation of the complete complex is essential for the proteasome to carry out its biochemical and physiological role in the parasite, namely to degrade specific target proteins in an ATP-dependent chaperone assisted manner ?
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Organism

Organism UniProt Comment Textmining
Plasmodium falciparum
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the HslUV complex is an assembly of heat shock locus gene products U and V. The formation of the complete complex is essential for the proteasome to carry out its biochemical and physiological role in the parasite, namely to degrade specific target proteins in an ATP-dependent chaperone assisted manner Plasmodium falciparum ?
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?

Subunits

Subunits Comment Organism
More the HslUV complex is an assembly of heat shock locus gene products U and V. The formation of the complete complex is essential for the proteasome to carry out its biochemical and physiological role in the parasite, namely to degrade specific target proteins in an ATP-dependent chaperone assisted manner. Homology modeling, molecular docking and computational alanine scanning to model the complex, are used to predict the binding mode of PfHslU-V interaction and to predict the binding-energy hot-spots in protein-protein interface, respectively Plasmodium falciparum

Synonyms

Synonyms Comment Organism
PfHslUV
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Plasmodium falciparum