ArticleJournal of structural biology2011
Structures of a key interaction protein from the Trypanosoma brucei editosome in complex with single domain antibodies.
Article in Journal of structural biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 29 citations in OpenAlex.
- KREPA6 functions in RNA editing catalytic complex structural organization and gRNA utilization in Trypanosoma brucei.Nucleic acids research · 2026Article
- Multiple domains of the integral KREPA3 protein are critical for the structure and precise functions of RNA editing catalytic complexes inRNA (New York, N.Y.) · 2023Article
- Structural basis of gRNA stabilization and mRNA recognition in trypanosomal RNA editing.Science (New York, N.Y.) · 2023Article
- Multiple domains of the integral KREPA3 protein are critical for the structure and precise functions of RNA Editing Catalytic Complexes inbioRxiv : the preprint server for biology · 2023Article
- Immunomodulation and Antioxidant Activities as Possible Trypanocidal and Cardioprotective Mechanisms of Major Terpenes fromAntioxidants (Basel, Switzerland) · 2021Article
- Biophysical insights from a single chain camelid antibody directed against the Disrupted-in-Schizophrenia 1 protein.PloS one · 2018Article
- Unveiling a Drift Resistant Cryptotope withinFrontiers in immunology · 2017Article
- Protein crystallization: Eluding the bottleneck of X-ray crystallography.AIMS biophysics · 2017Article
- Camelid Single-Domain Antibodies As an Alternative to Overcome Challenges Related to the Prevention, Detection, and Control of Neglected Tropical Diseases.Frontiers in immunology · 2017Review
- The Architecture of Trypanosoma brucei editosomes.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- U-Insertion/Deletion mRNA-Editing Holoenzyme: Definition in Sight.Trends in parasitology · 2016Review
- Comparison of the Mitochondrial Genomes and Steady State Transcriptomes of Two Strains of the Trypanosomatid Parasite, Leishmania tarentolae.PLoS neglected tropical diseases · 2015Article
- A general protocol for the generation of Nanobodies for structural biology.Nature protocols · 2014Article
- Article
- Explorations of linked editosome domains leading to the discovery of motifs defining conserved pockets in editosome OB-folds.Journal of structural biology · 2012Article
- The structure of the C-terminal domain of the largest editosome interaction protein and its role in promoting RNA binding by RNA-editing ligase L2.Nucleic acids research · 2012Article
- Antibody-enabled small-molecule drug discovery.Nature reviews. Drug discovery · 2012Review
- Crystal structure of a heterodimer of editosome interaction proteins in complex with two copies of a cross-reacting nanobody.Nucleic acids research · 2012Article
- The oligonucleotide binding (OB)-fold domain of KREPA4 is essential for stable incorporation into editosomes.PloS one · 2012Article
- Structural and functional studies on the interaction of GspC and GspD in the type II secretion system.PLoS pathogens · 2011Article
Corrections and comments
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Authors and funding
8 authors at 4 institutions in 2 countries.
Funding
Abstract
Several major global diseases are caused by single-cell parasites called trypanosomatids. These organisms exhibit many unusual features including a unique and essential U-insertion/deletion RNA editing process in their single mitochondrion. Many key RNA editing steps occur in ∼20S editosomes, which have a core of 12 proteins. Among these, the "interaction protein" KREPA6 performs a central role in maintaining the integrity of the editosome core and also binds to ssRNA. The use of llama single domain antibodies (VHH domains) accelerated crystal growth of KREPA6 from Trypanosoma brucei dramatically. All three structures obtained are heterotetramers with a KREPA6 dimer in the center, and one VHH domain bound to each KREPA6 subunit. Two of the resultant heterotetramers use complementarity determining region 2 (CDR2) and framework residues to form a parallel pair of beta strands with KREPA6 - a mode of interaction not seen before in VHH domain-protein antigen complexes. The third type of VHH domain binds in a totally different manner to KREPA6. Intriguingly, while KREPA6 forms tetramers in solution adding either one of the three VHH domains results in the formation of a heterotetramer in solution, in perfect agreement with the crystal structures. Biochemical solution studies indicate that the C-terminal tail of KREPA6 is involved in the dimerization of KREPA6 dimers to form tetramers. The implications of these crystallographic and solution studies for possible modes of interaction of KREPA6 with its many binding partners in the editosome are discussed.
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