ArticleBiochemical and biophysical research communications2014
Basic Tilted Helix Bundle - a new protein fold in human FKBP25/FKBP3 and HectD1.
Article in Biochemical and biophysical research communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 16 citations in OpenAlex.
- FKBP52 in Neuronal Signaling and Neurodegenerative Diseases: A Microtubule Story.International journal of molecular sciences · 2022Review
- Structural Insights into Ankyrin Repeat-Containing Proteins and Their Influence in Ubiquitylation.International journal of molecular sciences · 2021Review
- FKBP25 Regulates Meiotic Apparatus During Mouse Oocyte Maturation.Frontiers in cell and developmental biology · 2021Article
- The prolyl isomerase FKBP25 regulates microtubule polymerization impacting cell cycle progression and genomic stability.Nucleic acids research · 2018Article
- FKBP Ligands-Where We Are and Where to Go?Frontiers in pharmacology · 2018Review
- The basic tilted helix bundle domain of the prolyl isomerase FKBP25 is a novel double-stranded RNA binding module.Nucleic acids research · 2017Article
- Deletion of the N- or C-Terminal Helix of Apolipophorin III To Create a Four-Helix Bundle Protein.Biochemistry · 2016Article
- Structural basis of nucleic acid recognition by FK506-binding protein 25 (FKBP25), a nuclear immunophilin.Nucleic acids research · 2016Article
- Crystal structure of the FK506 binding domain of human FKBP25 in complex with FK506.Protein science : a publication of the Protein Society · 2016Article
- Prolyl isomerases in gene transcription.Biochimica et biophysica acta · 2015Review
- The prolyl isomerase, FKBP25, interacts with RNA-engaged nucleolin and the pre-60S ribosomal subunit.RNA (New York, N.Y.) · 2014Article
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Authors and funding
10 authors at 5 institutions in 2 countries.
Funding
Abstract
In this paper, we describe the structure of a N-terminal domain motif in nuclear-localized FKBP251-73, a member of the FKBP family, together with the structure of a sequence-related subdomain of the E3 ubiquitin ligase HectD1 that we show belongs to the same fold. This motif adopts a compact 5-helix bundle which we name the Basic Tilted Helix Bundle (BTHB) domain. A positively charged surface patch, structurally centered around the tilted helix H4, is present in both FKBP25 and HectD1 and is conserved in both proteins, suggesting a conserved functional role. We provide detailed comparative analysis of the structures of the two proteins and their sequence similarities, and analysis of the interaction of the proposed FKBP25 binding protein YY1. We suggest that the basic motif in BTHB is involved in the observed DNA binding of FKBP25, and that the function of this domain can be affected by regulatory YY1 binding and/or interactions with adjacent domains.
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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.