Literature summary for 4.2.1.96 extracted from

Rose, R.B.; Pullen, K.E.; Bayle, J.H.; Crabtree, G.R.; Alber, T.
Biochemical and structural basis for partially redundant enzymatic and transcriptional functions of DCoH and DCoH2 (2004), Biochemistry, 43, 7345-7355.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
hanging-drop vapor diffusion method at 4°C, 1.6 A resolution crystal structure, space group P3(1)21, unit cell length: a = b = 57.92 A, c = 114.63 A	Mus musculus

Organism

Organism	UniProt	Comment	Textmining
Mus musculus	Q9CZL5	DcoH2 (dimerization cofactor of HNF1alpha)	-

Purification (Commentary)

Purification (Comment)	Organism
DcoH2 (dimerization cofactor of HNF1alpha)	Mus musculus

Subunits

Subunits	Comment	Organism
tetramer	DcoH2 (dimerization cofactor of HNF1alpha), forms a tetramer, readily disproportionates and forms a 2:2 complex with HNF1 in vitro	Mus musculus

Synonyms

Synonyms	Comment	Organism
DcoH2	dimerization cofactor of HNF1alpha	Mus musculus

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Release 2023.1 (January 2023)