Structure of human cytidine deaminase bound to a potent inhibitor

Sang J. Chung; J. Christopher Fromme; Gregory L. Verdine

doi:10.1021/jm0496279

Structure of human cytidine deaminase bound to a potent inhibitor

Sang J. Chung, J. Christopher Fromme, Gregory L. Verdine

Research output: Contribution to journal › Article › peer-review

68 Scopus citations

Abstract

Human cytidine deaminase (CDA) is an enzyme prominent for its role in catalyzing metabolic processing of nucleoside-type anticancer and antiviral agents. It is thus a promising target for the development of small molecule therapeutic adjuvants. We report the first crystal structure of human CDA as a complex with a tight-binding inhibitor, diazepinone riboside 1. The structure reveals that inhibitor 1 is able to establish a canonical π/π-interaction with a key active site residue, Phe 137.

Original language	English
Pages (from-to)	658-660
Number of pages	3
Journal	Journal of Medicinal Chemistry
Volume	48
Issue number	3
DOIs	https://doi.org/10.1021/jm0496279
State	Published - 10 Feb 2005
Externally published	Yes

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abstract = "Human cytidine deaminase (CDA) is an enzyme prominent for its role in catalyzing metabolic processing of nucleoside-type anticancer and antiviral agents. It is thus a promising target for the development of small molecule therapeutic adjuvants. We report the first crystal structure of human CDA as a complex with a tight-binding inhibitor, diazepinone riboside 1. The structure reveals that inhibitor 1 is able to establish a canonical π/π-interaction with a key active site residue, Phe 137.",

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AU - Fromme, J. Christopher

AU - Verdine, Gregory L.

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N2 - Human cytidine deaminase (CDA) is an enzyme prominent for its role in catalyzing metabolic processing of nucleoside-type anticancer and antiviral agents. It is thus a promising target for the development of small molecule therapeutic adjuvants. We report the first crystal structure of human CDA as a complex with a tight-binding inhibitor, diazepinone riboside 1. The structure reveals that inhibitor 1 is able to establish a canonical π/π-interaction with a key active site residue, Phe 137.

AB - Human cytidine deaminase (CDA) is an enzyme prominent for its role in catalyzing metabolic processing of nucleoside-type anticancer and antiviral agents. It is thus a promising target for the development of small molecule therapeutic adjuvants. We report the first crystal structure of human CDA as a complex with a tight-binding inhibitor, diazepinone riboside 1. The structure reveals that inhibitor 1 is able to establish a canonical π/π-interaction with a key active site residue, Phe 137.

UR - https://www.scopus.com/pages/publications/13444265938

U2 - 10.1021/jm0496279

DO - 10.1021/jm0496279

M3 - Article

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EP - 660

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IS - 3

ER -

Structure of human cytidine deaminase bound to a potent inhibitor

Abstract

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