Literature summary for 1.14.11.68 extracted from

Sengoku, T.; Yokoyama, S.
Structural basis for histone H3 Lys 27 demethylation by UTX/KDM6A (2011), Genes Dev., 25, 2266-2277 .

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Crystallization (Commentary)

Crystallization (Comment)	Organism
crystal structures of the catalytic fragment of UTX/KDM6A, in the free and H3 peptide-bound forms. The catalytic jumonji domain binds H3 residues 25-33, recognizing H3R26, H3A29, and H3P30 in a sequence-specific manner, in addition to H3K27me3 in the catalytic pocket. A zinc-binding domain, conserved within the KDM6 family, binds residues 17-21 of H3. The zinc-binding domain changes its conformation upon H3 binding, and thereby recognizes the H3L20 side chain via a hydrophobic patch on its surface, which is inaccessible in the H3-free form. Residues H3R17, H3L20, H3R26, H3A29, H3P30, and H3T32 are each important for demethylation	Homo sapiens

Crystallization (Comment)

Organism

crystal structures of the catalytic fragment of UTX/KDM6A, in the free and H3 peptide-bound forms. The catalytic jumonji domain binds H3 residues 25-33, recognizing H3R26, H3A29, and H3P30 in a sequence-specific manner, in addition to H3K27me3 in the catalytic pocket. A zinc-binding domain, conserved within the KDM6 family, binds residues 17-21 of H3. The zinc-binding domain changes its conformation upon H3 binding, and thereby recognizes the H3L20 side chain via a hydrophobic patch on its surface, which is inaccessible in the H3-free form. Residues H3R17, H3L20, H3R26, H3A29, H3P30, and H3T32 are each important for demethylation

Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	O15550	-	-

Synonyms

Synonyms	Comment	Organism
KDM6A	-	Homo sapiens

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Release 2023.1 (January 2023)