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Literature DB >> 7583667

NMR structure of an inhibitory R2 C-terminal peptide bound to mouse ribonucleotide reductase R1 subunit.

Abstract

The structure of peptide N-AcYTLDADF when bound to the large subunit of mouse ribonucleotide reductase has been elucidated by transfer NOE. This structure suggests a general design for type 1 RR inhibitors.

Entities: Chemical Gene Species

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Year: 1995 PMID： 7583667 DOI： 10.1038/nsb1195-951

Source DB: PubMed Journal: Nat Struct Biol ISSN： 1072-8368

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Cited

6 in total

1. Structures of eukaryotic ribonucleotide reductase I define gemcitabine diphosphate binding and subunit assembly.

Authors: Hai Xu; Catherine Faber; Tomoaki Uchiki; Joseph Racca; Chris Dealwis
Journal: Proc Natl Acad Sci U S A Date: 2006-03-06 Impact factor: 11.205

2. The structural basis for peptidomimetic inhibition of eukaryotic ribonucleotide reductase: a conformationally flexible pharmacophore.

Authors: Hai Xu; James W Fairman; Sanath R Wijerathna; Nathan R Kreischer; John LaMacchia; Elizabeth Helmbrecht; Barry S Cooperman; Chris Dealwis
Journal: J Med Chem Date: 2008-07-09 Impact factor: 7.446

NMR structure of an inhibitory R2 C-terminal peptide bound to mouse ribonucleotide reductase R1 subunit.

1. Structures of eukaryotic ribonucleotide reductase I define gemcitabine diphosphate binding and subunit assembly.

2. The structural basis for peptidomimetic inhibition of eukaryotic ribonucleotide reductase: a conformationally flexible pharmacophore.

Review 3. The structural basis for the allosteric regulation of ribonucleotide reductase.

4. Targeting the Large Subunit of Human Ribonucleotide Reductase for Cancer Chemotherapy.

5. A novel clade of unique eukaryotic ribonucleotide reductase R2 subunits is exclusive to apicomplexan parasites.

6. A new set of atomic radii for accurate estimation of solvation free energy by Poisson-Boltzmann solvent model.