ArticleThe EMBO journal1995
Novel topology of a zinc-binding domain from a protein involved in regulating early Xenopus development.
Article in The EMBO journal, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- B1 oligomerization regulates PML nuclear body biogenesis and leukemogenesis.Nature communications · 2019Article
- Identification and functional characterization of the BBX24 promoter and gene from chrysanthemum in Arabidopsis.Plant molecular biology · 2015Article
- Evolutionary and Functional Analysis of Old World Primate TRIM5 Reveals the Ancient Emergence of Primate Lentiviruses and Convergent Evolution Targeting a Conserved Capsid Interface.PLoS pathogens · 2015Article
- Gain-of-sensitivity mutations in a Trim5-resistant primary isolate of pathogenic SIV identify two independent conserved determinants of Trim5α specificity.PLoS pathogens · 2013Article
- Involvement of the N-terminal B-box domain of Arabidopsis BBX32 protein in interaction with soybean BBX62 protein.The Journal of biological chemistry · 2012Article
- Article
- Nuclear localization and interaction with COP1 are required for STO/BBX24 function during photomorphogenesis.Plant physiology · 2011Article
- Functional diversification of the RING finger and other binuclear treble clef domains in prokaryotes and the early evolution of the ubiquitin system.Molecular bioSystems · 2011Article
- The vertebrate makorin ubiquitin ligase gene family has been shaped by large-scale duplication and retroposition from an ancestral gonad-specific, maternal-effect gene.BMC genomics · 2010Article
- The Arabidopsis B-box zinc finger family.The Plant cell · 2009Article
- Genomic analysis of the TRIM family reveals two groups of genes with distinct evolutionary properties.BMC evolutionary biology · 2008Article
- Interfering residues narrow the spectrum of MLV restriction by human TRIM5alpha.PLoS pathogens · 2007Article
- SALT TOLERANCE HOMOLOG2, a B-box protein in Arabidopsis that activates transcription and positively regulates light-mediated development.The Plant cell · 2007Article
- The control of viral infection by tripartite motif proteins and cyclophilin A.Retrovirology · 2007Review
- The tripartite motif of nuclear factor 7 is required for its association with transcriptional units.Molecular and cellular biology · 2007Article
- Functional replacement of the RING, B-box 2, and coiled-coil domains of tripartite motif 5alpha (TRIM5alpha) by heterologous TRIM domains.Journal of virology · 2006Article
- Structural classification of zinc fingers: survey and summary.Nucleic acids research · 2003Article
- Different modes of regulation of transcription and pre-mRNA processing of the structurally juxtaposed homologs, Rnf33 and Rnf35, in eggs and in pre-implantation embryos.Nucleic acids research · 2002Article
- PML protein isoforms and the RBCC/TRIM motif.Oncogene · 2001Review
- Solution structure of the PHD domain from the KAP-1 corepressor: structural determinants for PHD, RING and LIM zinc-binding domains.The EMBO journal · 2001Article
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Authors and funding
6 authors.
Funding
Abstract
Xenopus nuclear factor XNF7, a maternally expressed protein, functions in patterning of the embryo. XNF7 contains a number of defined protein domains implicated in the regulation of some developmental processes. Among these is a tripartite motif comprising a zinc-binding RING finger and B-box domain next to a predicted alpha-helical coiled-coil domain. Interestingly, this motif is found in a variety of protein including several proto-oncoproteins. Here we describe the solution structure of the XNF7 B-box zinc-binding domain determined at physiological pH by 1H NMR methods. The B-box structure represents the first three-dimensional structure of this new motif and comprises a monomer have two beta-strands, two helical turns and three extended loop regions packed in a novel topology. The r.m.s. deviation for the best 18 structures is 1.15 A for backbone atoms and 1.94 A for all atoms. Structure calculations and biochemical data shows one zinc atom ligated in a Cys2-His2 tetrahedral arrangement. We have used mutant peptides to determine the metal ligation scheme which surprisingly shows that not all of the seven conserved cysteines/histidines in the B-box motif are involved in metal ligation. The B-box structure is not similar in tertiary fold to any other known zinc-binding motif.
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