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Crystal Structure of Human Indoleamine 2,3-Dioxygenase: Catalytic Mechanism of O₂ Incorporation by a...

Crystal Structure of Human Indoleamine 2,3-Dioxygenase: Catalytic Mechanism of O₂ Incorporation by a...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_1413787

Crystal Structure of Human Indoleamine 2,3-Dioxygenase: Catalytic Mechanism of O₂ Incorporation by a Heme-Containing Dioxygenase

About this item

Full title

Crystal Structure of Human Indoleamine 2,3-Dioxygenase: Catalytic Mechanism of O₂ Incorporation by a Heme-Containing Dioxygenase

Publisher

United States: National Academy of Sciences

Journal title

Proceedings of the National Academy of Sciences - PNAS, 2006-02, Vol.103 (8), p.2611-2616

Language

English

Formats

Publication information

Publisher

United States: National Academy of Sciences

More information

Scope and Contents

Contents

Human indoleamine 2,3-dioxygenase (IDO) catalyzes the cleavage of the pyrrol ring of L-Trp and incorporates both atoms of a molecule of oxygen (O₂). Here we report on the x-ray crystal structure of human IDO, complexed with the ligand inhibitor 4-phenylimidazole and cyanide. The overall structure of IDO shows two a-helical domains with the heme bet...

Alternative Titles

Full title

Crystal Structure of Human Indoleamine 2,3-Dioxygenase: Catalytic Mechanism of O₂ Incorporation by a Heme-Containing Dioxygenase

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_1413787

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_1413787

Other Identifiers

ISSN

0027-8424

E-ISSN

1091-6490

DOI

10.1073/pnas.0508996103

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