ArticleProceedings of the National Academy of Sciences of the United States of America1996
Metal binding properties and secondary structure of the zinc-binding domain of Nup475.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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34 citing papers in PubMed, 102 citations in OpenAlex.
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- Zinc-Chelating Mechanism of Sea Cucumber (Marine drugs · 2019Article
- The tandem zinc finger RNA binding domain of members of the tristetraprolin protein family.Wiley interdisciplinary reviews. RNA · 2019Review
- Co(II) Coordination in Prokaryotic Zinc Finger Domains as Revealed by UV-Vis Spectroscopy.Bioinorganic chemistry and applications · 2017Article
- Three Residues Make an Evolutionary Switch for Folding and RNA-Destabilizing Activity in the TTP Family of Proteins.ACS chemical biology · 2016Article
- Probing the structural and dynamical effects of the charged residues of the TZF domain of TIS11d.Biophysical journal · 2015Article
- The Arabidopsis thaliana tandem zinc finger 1 (AtTZF1) protein in RNA binding and decay.The Plant journal : for cell and molecular biology · 2014Article
- Protein design: toward functional metalloenzymes.Chemical reviews · 2014Review
- Switching metal ion coordination and DNA Recognition in a Tandem CCHHC-type zinc finger peptide.Inorganic chemistry · 2013Article
- Evidence that highly conserved residues of transmembrane segment 6 of Escherichia coli MntH are important for transport activity.Biochemistry · 2010Article
- Inactivation of respiratory syncytial virus by zinc finger reactive compounds.Virology journal · 2010Article
- The respiratory syncytial virus M2-1 protein forms tetramers and interacts with RNA and P in a competitive manner.Journal of virology · 2009Article
- Inhibition of tristetraprolin deadenylation by poly(A) binding protein.American journal of physiology. Gastrointestinal and liver physiology · 2008Article
- Substrate dependence of conformational changes in the RNA-binding domain of tristetraprolin assessed by fluorescence spectroscopy of tryptophan mutants.Biochemistry · 2006Article
- Functional analysis of the RING-type ubiquitin ligase family of Arabidopsis.Plant physiology · 2005Article
- Article
- The splicing factor U2AF small subunit is functionally conserved between fission yeast and humans.Molecular and cellular biology · 2004Article
- Expression and purification of recombinant tristetraprolin that can bind to tumor necrosis factor-alpha mRNA and serve as a substrate for mitogen-activated protein kinases.Archives of biochemistry and biophysics · 2003Article
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4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nup475 is a nuclear zinc-binding protein of unknown function that is induced in mammalian cells by growth factor mitogens. Nup475 contains two tandemly repeated sequences YKTELCX8CX5CX3H (Cys3His repeats) that are thought to be zinc-bindin domains. Similar sequences have been found in a number of proteins from various species of eukaryotes. To determine the metal binding properties and secondary structure of the putative zinc-binding domains of Nup475, we have used synthetic or recombinant peptides that contain one or two domain sequences. The peptide with a single domain bound 1.0 +/- 0.1 equivalents of Co2+, and the peptide with two domains bound 1.7 +/- 0.4 equivalents of Co2+. Both peptides bound Co2+ and Zn2+ with affinities similar to those of classical zinc finger peptides. In each case, the Co2+ complex exhibited strong d-d transitions characteristic of tetrahedral coordination. For structural studies by nuclear magnetic resonance spectroscopy, we used a more soluble two-domain peptide that had a single amino acid substitution in a nonconserved amino acid residue in the second Cys3His repeat. The mutant peptide unexpectedly showed loss of one of its metal binding sites and displayed ordered structure for only the first Cys3His sequence. On the basis of the nuclear magnetic resonance data, we propose a structure for the Nup475 metal-binding domain in which the zinc ion is coordinated by the conserved cysteines and histidine, and the conserved YKTEL motif forms a parallel sheet-like structure with the C terminus of this domain. This structure is unlike that of any previously described class of metal binding domain.
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