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Literature summary for 3.4.24.36 extracted from

  • Bianchini, G.; Bocedi, A.; Ascenzi, P.; Gavuzzo, E.; Mazza, F.; Aschi, M.
    Molecular dynamics simulation of Leishmania major surface metalloprotease GP63 (leishmanolysin) (2006), Proteins, 64, 385-390.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
molecular dynamics simulation of enzyme in water. Upon solvation, enzyme undergoes a sharp structural relaxation with respect to the crystal structure. Fingerprint fluctuations of enzyme are characterized by the motion of a large part of the N-terminal domain, which is also involved in substrate recognition and proenzyme activation. Residues involved in interdomain binding are highly conserved Leishmania major

Organism

Organism UniProt Comment Textmining
Leishmania major
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