Title : Structural analysis of CYP2R1 in complex with vitamin D3.

Pub. Date : 2008 Jun 27

PMID : 18511070






4 Functional Relationships(s)
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1 Structural analysis of CYP2R1 in complex with vitamin D3. Cholecalciferol cytochrome P450 family 2 subfamily R member 1 Homo sapiens
2 To understand the narrow substrate specificity of CYP2R1 we obtained the hemeprotein in a highly purified state, confirmed the enzyme as a vitamin D 25-hydroxylase, and solved the crystal structure of CYP2R1 in complex with vitamin D3. Cholecalciferol cytochrome P450 family 2 subfamily R member 1 Homo sapiens
3 To understand the narrow substrate specificity of CYP2R1 we obtained the hemeprotein in a highly purified state, confirmed the enzyme as a vitamin D 25-hydroxylase, and solved the crystal structure of CYP2R1 in complex with vitamin D3. Cholecalciferol cytochrome P450 family 2 subfamily R member 1 Homo sapiens
4 To understand the narrow substrate specificity of CYP2R1 we obtained the hemeprotein in a highly purified state, confirmed the enzyme as a vitamin D 25-hydroxylase, and solved the crystal structure of CYP2R1 in complex with vitamin D3. Cholecalciferol cytochrome P450 family 2 subfamily R member 1 Homo sapiens