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Structural basis for allosteric regulation of human ribonucleotide reductase by nucleotide-induced o...

Structural basis for allosteric regulation of human ribonucleotide reductase by nucleotide-induced o...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_swepub_primary_oai_swepub_ki_se_546014

Structural basis for allosteric regulation of human ribonucleotide reductase by nucleotide-induced oligomerization

About this item

Full title

Structural basis for allosteric regulation of human ribonucleotide reductase by nucleotide-induced oligomerization

Publisher

New York: Nature Publishing Group US

Journal title

Nature structural & molecular biology, 2011-03, Vol.18 (3), p.316-322

Language

English

Formats

Publication information

Publisher

New York: Nature Publishing Group US

More information

Scope and Contents

Contents

Ribonucleotide reductase is essential to maintain the cellular pools of dNTPs, and its activity is controlled allosterically by ATP (activator) and dATP (inhibitor). Now crystal and EM structures of human and yeast ribonucleotide reductase 1 in complex with different nucleotides, together with mutagenesis and functional analysis, reveal how dATP bi...

Alternative Titles

Full title

Structural basis for allosteric regulation of human ribonucleotide reductase by nucleotide-induced oligomerization

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_swepub_primary_oai_swepub_ki_se_546014

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_swepub_primary_oai_swepub_ki_se_546014

Other Identifiers

ISSN

1545-9993,1545-9985

E-ISSN

1545-9985

DOI

10.1038/nsmb.2007