ArticleStructure (London, England : 1993)2007
Structure of the calcineurin-NFAT complex: defining a T cell activation switch using solution NMR and crystal coordinates.
Article in Structure (London, England : 1993), 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 54 citations in OpenAlex.
- DYRK1A and Parkinson's disease, facts and hypotheses.Neurobiology of disease · 2026Review
- Role of the Alpha-B-Crystallin Protein in Cardiomyopathic Disease.International journal of molecular sciences · 2024Review
- Funneling modulatory peptide design with generative models: Discovery and characterization of disruptors of calcineurin protein-protein interactions.PLoS computational biology · 2023Article
- Targeting CaN/NFAT in Alzheimer's brain degeneration.Frontiers in immunology · 2023Review
- The optimized core peptide derived from CABIN1 efficiently inhibits calcineurin-mediated T-cell activation.Experimental & molecular medicine · 2022Article
- Leveraging New Definitions of the LxVP SLiM To Discover Novel Calcineurin Regulators and Substrates.ACS chemical biology · 2019Article
- Calmodulin-Calcineurin Interaction beyond the Calmodulin-Binding Region Contributes to Calcineurin Activation.Biochemistry · 2019Article
- Investigating the human Calcineurin Interaction Network using the πɸLxVP SLiM.Scientific reports · 2016Article
- The Emerging Roles of the Calcineurin-Nuclear Factor of Activated T-Lymphocytes Pathway in Nervous System Functions and Diseases.Journal of aging research · 2016Review
- Short linear motifs - ex nihilo evolution of protein regulation.Cell communication and signaling : CCS · 2015Review
- NMR resonance assignments of the catalytic domain of human serine/threonine phosphatase calcineurin in unligated and PVIVIT-peptide-bound states.Biomolecular NMR assignments · 2015Article
- Calcineurin Undergoes a Conformational Switch Evoked via Peptidyl-Prolyl Isomerization.PloS one · 2015Article
- Structure-based optimization of a peptidyl inhibitor against calcineurin-nuclear factor of activated T cell (NFAT) interaction.Journal of medicinal chemistry · 2014Article
- The LxVP and PxIxIT NFAT motifs bind jointly to overlapping epitopes on calcineurin's catalytic domain distant to the regulatory domain.Structure (London, England : 1993) · 2014Article
- Calcineurin interacts with the serotonin transporter C-terminus to modulate its plasma membrane expression and serotonin uptake.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2013Article
- Functional diversity and pharmacological profiles of the FKBPs and their complexes with small natural ligands.Cellular and molecular life sciences : CMLS · 2013Review
- The molecular mechanism of substrate engagement and immunosuppressant inhibition of calcineurin.PLoS biology · 2013Article
- Balanced interactions of calcineurin with AKAP79 regulate Ca2+-calcineurin-NFAT signaling.Nature structural & molecular biology · 2012Article
- The Crz1/Sp1 transcription factor of Cryptococcus neoformans is activated by calcineurin and regulates cell wall integrity.PloS one · 2012Article
- Observation of intermolecular interactions in large protein complexes by 2D-double difference nuclear Overhauser enhancement spectroscopy: application to the 44 kDa interferon-receptor complex.Journal of the American Chemical Society · 2011Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Calcineurin (Cn) is a serine/threonine protein phosphatase that plays pivotal roles in many physiological processes, including cell proliferation, development, and apoptosis. Most prominently, Cn targets the nuclear factors of activated T cell (NFATs), transcription factors that activate cytokine genes. Calcium-activated Cn dephosphorylates multiple residues within the regulatory domain of NFAT, triggering joint nuclear translocation. This relies crucially on the interaction between the catalytic domain of Cn (CnCat) and the conserved PxIxIT motif located in a region distinct from the dephosphorylation sites of NFAT. Here, we present the structure of the complex between the 39 kDa CnCat and a 14 residue peptide containing a PVIVIT segment that was derived from affinity-driven peptide selection based on the conserved PxIxIT motif of NFATs. The structure of the complex was determined by using NMR assignments and structural constraints and the coordinates of the CnCat crystal structure. The NMR analysis relied on recently developed labeling and spectroscopic techniques. The VIVIT peptide is accommodated in a hydrophobic cleft formed by beta strands 11 and 14, and the loop between beta strands 11 and 12, forming a short parallel beta sheet with the exposed beta strand 14 in Cn. The side chains of conserved residues in the PxIxIT sequences make extensive interactions with conserved residues in Cn, while those of nonconserved residues are solvent exposed. The architecture of the interface explains the diversity of recognition sequences compatible with NFAT function and uncovers a potential targeting site for immune-suppressive agents. The structure reveals that the orientation of the bound PxIxIT directs the phosphorylation sites in NFAT's regulatory domain toward the Cn catalytic site.
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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.