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Literature summary for 3.4.14.4 extracted from

  • Tomic, A.; Gonzalez, M.; Tomic, S.
    The large scale conformational change of the human DPP III-substrate prefers the "closed" form (2012), J. Chem. Inf. Model., 52, 1583-1594.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
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Homo sapiens

Protein Variants

Protein Variants Comment Organism
D372A residue Asp372 plays a crucial role in the large scale interdomain closure. During the MD simulation time, the variant remains more open than the wild type protein. Apparently, Ala is not as efficient as Asp in establishing the interdomain interactions Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens Q9NY33
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-Arg-L-Arg-2-naphthylamide + H2O binding free energy calculations reveal tighter binding of the preferred synthetic substrate Arg-Arg-2-naphtylamide to the closed than to the open enzyme conformation. The electrostatic component of the free energy of solvation is higher for the closed protein than for its less compact form Homo sapiens L-Arg-L-Arg + 2-naphthylamine
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