ArticleNucleic acids research2010
Structure of Smad1 MH1/DNA complex reveals distinctive rearrangements of BMP and TGF-beta effectors.
Article in Nucleic acids research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
48 citing papers in PubMed, 69 citations in OpenAlex.
- Structural basis of Nuclear Factor 1-X DNA recognition provides prototypic insight into the NFI family.Nature communications · 2025Article
- Drosophila Dpp and BMP signaling directly regulates dpp transcription for optimal ligand production.Development (Cambridge, England) · 2025Article
- Bimodal specificity of TF-DNA recognition in embryonic stem cells.Nucleic acids research · 2025Article
- Article
- Cooperative Gsx2-DNA binding requires DNA bending and a novel Gsx2 homeodomain interface.Nucleic acids research · 2024Article
- Evaluation of the determinants for improved pluripotency induction and maintenance by engineered SOX17.Nucleic acids research · 2023Article
- Fluid shear stress-modulated chromatin accessibility reveals the mechano-dependency of endothelial SMAD1/5-mediated gene transcription.iScience · 2023Article
- Article
- The homeodomain of Oct4 is a dimeric binder of methylated CpG elements.Nucleic acids research · 2023Article
- SOX9 and SOX10 control fluid homeostasis in the inner ear for hearing through independent and cooperative mechanisms.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- FOXL2 and FOXA1 cooperatively assemble on the TP53 promoter in alternative dimer configurations.Nucleic acids research · 2022Article
- Anti-Müllerian Hormone Signal Transduction involved in Müllerian Duct Regression.Frontiers in endocrinology · 2022Review
- Jiawei Yanghe Decoction Regulates Bone-Lipid Balance through the BMP-SMAD Signaling Pathway to Promote Osteogenic Differentiation of Bone Mesenchymal Stem Cells.Evidence-based complementary and alternative medicine : eCAM · 2022Article
- Bmp Signaling Regulates Hand1 in a Dose-Dependent Manner during Heart Development.International journal of molecular sciences · 2021Article
- HumanCardiogenetics · 2021Article
- Human cytomegalovirus blocks canonical TGFβ signaling during lytic infection to limit induction of type I interferons.PLoS pathogens · 2021Article
- Mechanism of forkhead transcription factors binding to a novel palindromic DNA site.Nucleic acids research · 2021Article
- The BMP signaling gradient is interpreted through concentration thresholds in dorsal-ventral axial patterning.PLoS biology · 2021Article
- Unveiling the dimer/monomer propensities of Smad MH1-DNA complexes.Computational and structural biotechnology journal · 2021Article
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Smad1 is a downstream effector of the BMP signaling pathway that binds regulatory DNA to execute gene expression programs leading to, for example, the maintenance of pluripotency in mice. On the contrary, the TGF-beta-activated Smad3 triggers strikingly different programs such as mesodermal differentiation in early development. Because Smad1 and Smad3 contain identical amino acids at the DNA contact interface it is unclear how they elicit distinctive bioactivities. Here, we report the crystal structure of the MH1 domain of Smad1 bound to a palindromic Smad binding element. Surprisingly, the DNA contact interface of Smad1 is drastically rearranged when compared to Smad3. The N-terminal helix 1 of Smad1 is dislodged from its intramolecular binding site and adopts a domain swapped arrangement with a symmetry-related molecule. As a consequence, helix 2 kinks away from the double helix disabling several key phosphate backbone interactions. Thermal melting analysis corroborates a decompacted conformation of Smad1 and DNA binding assays indicate a lower overall affinity of Smad1 to DNA but increased cooperativity when binding to palindromic DNA motifs. These findings suggest that Smad1 and Smad3 evolved differential qualities to assemble on composite DNA elements and to engage in co-factor interactions by remodeling their N-termini.
Indexed as
Identifiers
What OpenQuestion holds
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.