ArticleActa crystallographica. Section D, Biological crystallography2014
Structures of the NLRP14 pyrin domain reveal a conformational switch mechanism regulating its molecular interactions.
Article in Acta crystallographica. Section D, Biological crystallography, 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, 21 citations in OpenAlex.
- Unraveling the Molecular Mechanisms of Activated Protein C (APC) in Mitigating Reperfusion Injury and Cardiac Ischemia: a Promising Avenue for Novel Therapeutic Interventions.Journal of cardiovascular translational research · 2024Review
- Directionality of PYD filament growth determined by the transition of NLRP3 nucleation seeds to ASC elongation.Science advances · 2022Article
- Impact of linker histone in the formation of ambochlorin-calf thymus DNA complex: Multi-spectroscopic, stopped-flow, and molecular modeling approaches.Iranian journal of basic medical sciences · 2021Article
- Assembly of platforms for signal transduction in the new era: dimerization, helical filament assembly, and beyond.Experimental & molecular medicine · 2020Review
- Structural basis for dimerization of the death effector domain of the F122A mutant of Caspase-8.Scientific reports · 2018Article
- Microarray and whole-exome sequencing analysis of familial Behçet's disease patients.Scientific reports · 2016Article
- Activation and assembly of the inflammasomes through conserved protein domain families.Apoptosis : an international journal on programmed cell death · 2015Review
- Intrinsic flexibility of NLRP pyrin domains is a key factor in their conformational dynamics, fold stability, and dimerization.Protein science : a publication of the Protein Society · 2015Article
- An updated view on the structure and function of PYRIN domains.Apoptosis : an international journal on programmed cell death · 2015Article
- International Union of Basic and Clinical Pharmacology. XCVI. Pattern recognition receptors in health and disease.Pharmacological reviews · 2015Review
- Structural mechanisms in NLR inflammasome signaling.Current opinion in structural biology · 2014Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The cytosolic tripartite NLR receptors serve as important signalling platforms in innate immunity. While the C-terminal domains act as sensor and activation modules, the N-terminal death-like domain, e.g. the CARD or pyrin domain, is thought to recruit downstream effector molecules by homotypic interactions. Such homotypic complexes have been determined for all members of the death-domain superfamily except for pyrin domains. Here, crystal structures of human NLRP14 pyrin-domain variants are reported. The wild-type protein as well as the clinical D86V mutant reveal an unexpected rearrangement of the C-terminal helix α6, resulting in an extended α5/6 stem-helix. This reordering mediates a novel symmetric pyrin-domain dimerization mode. The conformational switching is controlled by a charge-relay system with a drastic impact on protein stability. How the identified charge relay allows classification of NLRP receptors with respect to distinct recruitment mechanisms is discussed.
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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.