Literature summary for 3.5.1.98 extracted from

Guo, L.; Han, A.; Bates, D.L.; Cao, J.; Chen, L.
Crystal structure of a conserved N-terminal domain of histone deacetylase 4 reveals functional insights into glutamine-rich domains (2007), Proc. Natl. Acad. Sci. USA, 104, 4297-4302.

Crystallization (Commentary)

Crystallization (Comment)	Organism
N-terminal glutamine-rich fragment, residues 62-153. The glutamine-rich domain folds into an alpha-helix that assembles as a tetramer lacking regularly arranged apolar residues and an extended hydrophobic core. Instead, the protein interfaces consist of multiple hydrophobic patches interspersed with polar interaction networks, wherein clusters of glutamines engage in extensive intra- and interhelical interactions. In solution, the tetramer undergoes rapid equilibrium with monomer and intermediate species	Homo sapiens

Crystallization (Comment)

Organism

N-terminal glutamine-rich fragment, residues 62-153. The glutamine-rich domain folds into an alpha-helix that assembles as a tetramer lacking regularly arranged apolar residues and an extended hydrophobic core. Instead, the protein interfaces consist of multiple hydrophobic patches interspersed with polar interaction networks, wherein clusters of glutamines engage in extensive intra- and interhelical interactions. In solution, the tetramer undergoes rapid equilibrium with monomer and intermediate species

Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P56524	isoform HDAC4	-

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Release 2023.1 (January 2023)