2hi4: Difference between revisions

Revision as of 20:10, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2hi4.png

Template:STRUCTURE 2hi4

Crystal Structure of Human Microsomal P450 1A2 in complex with alpha-naphthoflavoneCrystal Structure of Human Microsomal P450 1A2 in complex with alpha-naphthoflavone

Template:ABSTRACT PUBMED 17311915

About this StructureAbout this Structure

2HI4 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Adaptations for the oxidation of polycyclic aromatic hydrocarbons exhibited by the structure of human P450 1A2., Sansen S, Yano JK, Reynald RL, Schoch GA, Griffin KJ, Stout CD, Johnson EF, J Biol Chem. 2007 May 11;282(19):14348-55. Epub 2007 Feb 20. PMID:17311915

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Crystal Structure of Human Microsomal P450 1A2 in complex with alpha-naphthoflavone'''
+===Crystal Structure of Human Microsomal P450 1A2 in complex with alpha-naphthoflavone===
-==Overview==
+<!--
-Microsomal cytochrome P450 family 1 enzymes play prominent roles in xenobiotic detoxication and procarcinogen activation. P450 1A2 is the principal cytochrome P450 family 1 enzyme expressed in human liver and participates extensively in drug oxidations. This enzyme is also of great importance in the bioactivation of mutagens, including the N-hydroxylation of arylamines. P450-catalyzed reactions involve a wide range of substrates, and this versatility is reflected in a structural diversity evident in the active sites of available P450 structures. Here, we present the structure of human P450 1A2 in complex with the inhibitor alpha-naphthoflavone, determined to a resolution of 1.95 A. alpha-Naphthoflavone is bound in the active site above the distal surface of the heme prosthetic group. The structure reveals a compact, closed active site cavity that is highly adapted for the positioning and oxidation of relatively large, planar substrates. This unique topology is clearly distinct from known active site architectures of P450 family 2 and 3 enzymes and demonstrates how P450 family 1 enzymes have evolved to catalyze efficiently polycyclic aromatic hydrocarbon oxidation. This report provides the first structure of a microsomal P450 from family 1 and offers a template to study further structure-function relationships of alternative substrates and other cytochrome P450 family 1 members.
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+{{ABSTRACT_PUBMED_17311915}}
 ==About this Structure==
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 [[Category: P450]]
 [[Category: P450 1a2]]
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