ArticleProtein science : a publication of the Protein Society2008
Crystallographic and biochemical studies revealing the structural basis for antizyme inhibitor function.
Article in Protein science : a publication of the Protein Society, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 43 citations in OpenAlex.
- Article
- Article
- Polyamines: Functions, Metabolism, and Role in Human Disease Management.Medical sciences (Basel, Switzerland) · 2021Review
- Polyamine synthesis as a target ofThe Journal of biological chemistry · 2018Review
- The antizyme family for regulating polyamines.The Journal of biological chemistry · 2018Review
- Antizyme Inhibitors in Polyamine Metabolism and Beyond: Physiopathological Implications.Medical sciences (Basel, Switzerland) · 2018Review
- Myc, Oncogenic Protein Translation, and the Role of Polyamines.Medical sciences (Basel, Switzerland) · 2018Review
- Antizyme inhibitor 1: a potential carcinogenic molecule.Cancer science · 2017Review
- Multifaceted interactions and regulation between antizyme and its interacting proteins cyclin D1, ornithine decarboxylase and antizyme inhibitor.Oncotarget · 2015Article
- Structural basis of antizyme-mediated regulation of polyamine homeostasis.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Translational development of difluoromethylornithine (DFMO) for the treatment of neuroblastoma.Translational pediatrics · 2015Review
- Novel interaction of ornithine decarboxylase with sepiapterin reductase regulates neuroblastoma cell proliferation.Journal of molecular biology · 2014Article
- Article
- Structural and degradative aspects of ornithine decarboxylase antizyme inhibitor 2.FEBS open bio · 2014Article
- Recoding RNA editing of AZIN1 predisposes to hepatocellular carcinoma.Nature medicine · 2013Article
- Structural insight into DFMO resistant ornithine decarboxylase from Entamoeba histolytica: an inkling to adaptive evolution.PloS one · 2013Article
- Article
- Polyamine pathway inhibition as a novel therapeutic approach to treating neuroblastoma.Frontiers in oncology · 2012Article
- Biochemical, mutational and in silico structural evidence for a functional dimeric form of the ornithine decarboxylase from Entamoeba histolytica.PLoS neglected tropical diseases · 2012Article
- Evidence of a role for antizyme and antizyme inhibitor as regulators of human cancer.Molecular cancer research : MCR · 2011Review
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Antizyme inhibitor (AzI) regulates cellular polyamine homeostasis by binding to the polyamine-induced protein, Antizyme (Az), with greater affinity than ornithine decarboxylase (ODC). AzI is highly homologous to ODC but is not enzymatically active. In order to understand these specific characteristics of AzI and its differences from ODC, we determined the 3D structure of mouse AzI to 2.05 A resolution. Both AzI and ODC crystallize as a dimer. However, fewer interactions at the dimer interface, a smaller buried surface area, and lack of symmetry of the interactions between residues from the two monomers in the AzI structure suggest that this dimeric structure is nonphysiological. In addition, the absence of residues and interactions required for pyridoxal 5'-phosphate (PLP) binding suggests that AzI does not bind PLP. Biochemical studies confirmed the lack of PLP binding and revealed that AzI exists as a monomer in solution while ODC is dimeric. Our findings that AzI exists as a monomer and is unable to bind PLP provide two independent explanations for its lack of enzymatic activity and suggest the basis for its enhanced affinity toward Az.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.