NDLI: Crystal structure of the human ecto-5'-nucleotidase (CD73): insights into the regulation of purinergic signaling.

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Crystal structure of the human ecto-5'-nucleotidase (CD73): insights into the regulation of purinergic signaling.

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Crystal structure of the human ecto-5'-nucleotidase (CD73): insights into the regulation of purinergic signaling.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Knapp, Karen Zebisch, Matthias Pippel, Jan El-Tayeb, Ali Müller, Christa E. Sträter, Norbert
Description	Country affiliation: Germany Author Affiliation: Knapp K ( Institute of Bioanalytical Chemistry, Center for Biotechnology and Biomedicine, University of Leipzig, Deutscher Platz 5, 04103 Leipzig, Germany.)
Abstract	In vertebrates ecto-5'-nucleotidase (e5NT) catalyzes the hydrolysis of extracellular AMP to adenosine and represents the major control point for extracellular adenosine levels. Due to its pivotal role for activation of P1 adenosine receptors, e5NT has emerged as an appealing drug target for treatment of inflammation, chronic pain, hypoxia, and cancer. Crystal structures of the dimeric human e5NT reveal an extensive 114° conformational switch between the open and closed forms of the enzyme. The dimerization interface is formed by the C-terminal domains and exhibits interchain motions of up to 13°. Complex structures with adenosine and AMPCP indicate that structural control of the domain movement determines the selectivity for monophosphate nucleotides. Binding modes of nucleotide-derived and flavonoid-based compounds complexed to the C-terminal domain in the open form reveal an additional binding pocket of â¼210 Å(3) that might be explored to design more potent inhibitors.
File Format	HTM / HTML
ISSN	09692126
Issue Number	12
Volume Number	20
e-ISSN	18784186
Journal	Structure
Language	English
Publisher	Elsevier
Publisher Date	2012-12-05
Publisher Place	United States
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Discipline Molecular Biology Discipline Biochemistry Discipline Biotechnology 5'-nucleotidase Chemistry Signal Transduction Antagonists & Inhibitors Adenosine Adenosine Diphosphate Analogs & Derivatives Amino Acid Sequence Catalytic Domain Coordination Complexes Crystallography, X-ray Enzyme Inhibitors Flavonoids Gpi-linked Proteins Humans Hydrogen Bonding Hydrophobic And Hydrophilic Interactions Models, Molecular Molecular Sequence Data Protein Binding Protein Interaction Domains And Motifs Protein Structure, Quaternary Protein Structure, Secondary Protein Subunits Structural Homology, Protein Zinc Journal Article Research Support, Non-u.s. Gov't
Content Type	Text
Resource Type	Article
Subject	Structural Biology Molecular Biology

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The Ecto-5’-Nucleotidase/CD73 Inhibitor, α,β-Methylene Adenosine 5’-Diphosphate, Exacerbates Carrageenan-Induced Pleurisy in Rat

Allergen-induced airway hyperresponsiveness is absent in ecto-5′-nucleotidase (CD73)-deficient mice

Ecto-5’-nucleotidase: Structure function relationships

Superior working memory and behavioural habituation but diminished psychomotor coordination in mice lacking the ecto-5′-nucleotidase (CD73) gene

Exacerbation of Allergic Airway Inflammation in Mice Lacking ECTO-5′-Nucleotidase (CD73)

Insights into Cullin-RING E3 ubiquitin ligase recruitment: structure of the VHL-EloBC-Cul2 complex.

NTPDase3 and ecto-5′-nucleotidase/CD73 are differentially expressed during mouse bladder cancer progression

Activity and expression of ecto-5′-nucleotidase/CD73 are increased by thyroid hormones in vascular smooth muscle cells

High expression and activity of ecto-5′-nucleotidase/CD73 in the male murine reproductive tract

Crystal structure of the human ecto-5'-nucleotidase (CD73): insights into the regulation of purinergic signaling.

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The Ecto-5’-Nucleotidase/CD73 Inhibitor, α,β-Methylene Adenosine 5’-Diphosphate, Exacerbates Carrageenan-Induced Pleurisy in Rat

Allergen-induced airway hyperresponsiveness is absent in ecto-5′-nucleotidase (CD73)-deficient mice

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Superior working memory and behavioural habituation but diminished psychomotor coordination in mice lacking the ecto-5′-nucleotidase (CD73) gene

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Activity and expression of ecto-5′-nucleotidase/CD73 are increased by thyroid hormones in vascular smooth muscle cells

High expression and activity of ecto-5′-nucleotidase/CD73 in the male murine reproductive tract

Crystal structure of the human ecto-5'-nucleotidase (CD73): insights into the regulation of purinergic signaling.