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BRENDA support

Literature summary for 2.3.1.286 extracted from

  • Yamagata, K.; Goto, Y.; Nishimasu, H.; Morimoto, J.; Ishitani, R.; Dohmae, N.; Takeda, N.; Nagai, R.; Komuro, I.; Suga, H.; Nureki, O.
    Structural basis for potent inhibition of SIRT2 deacetylase by a macrocyclic peptide inducing dynamic structural change (2014), Structure, 22, 345-352.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
crystallization at 4°C by the sitting-drop vapor diffusion method. Crystal structure of human SIRT2 in complex with a macrocyclic peptide inhibitor S2iL5, at 2.5 A resolution Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
macrocyclic peptide inhibitor S2iL5 the inhibitor binds to the active site of SIRT2 through extensive interactions. The inhibitor induces an open-to-closed domain movement and a helix-to-coil transition in a SIRT2-specific region Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens Q8IXJ6
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Homo sapiens

Synonyms

Synonyms Comment Organism
SIRT2
-
Homo sapiens