PlantImRecepV1, Main, Exploration, bibRecord, 000222

A survey of TIR domain sequence and structure divergence.

Identifieur interne : 000222 ( Main/Exploration ); précédent : 000221; suivant : 000223

A survey of TIR domain sequence and structure divergence.

Auteurs : Vladimir Y. Toshchakov [États-Unis] ; Andrew F. Neuwald [États-Unis]

Source :

Immunogenetics [ 1432-1211 ] ; 2020.

RBID : pubmed:32002590

Descripteurs français

KwdFr :
- Animaux (MeSH), Bases de données génétiques (MeSH), Domaines protéiques (génétique), Domaines protéiques (physiologie), Facteur de différenciation myéloïde-88 (génétique), Facteur de différenciation myéloïde-88 (métabolisme), Humains (MeSH), Interleukines (MeSH), Modèles moléculaires (MeSH), Protéines adaptatrices de la transduction du signal (génétique), Protéines adaptatrices de la transduction du signal (métabolisme), Protéines de Drosophila (génétique), Protéines de Drosophila (métabolisme), Récepteurs de type Toll (génétique), Récepteurs de type Toll (métabolisme), Récepteurs à l'interleukine-1 (génétique), Récepteurs à l'interleukine-1 (métabolisme), Structure secondaire des protéines (MeSH), Séquence d'acides aminés (MeSH), Théorème de Bayes (MeSH), Transduction du signal (génétique), Transduction du signal (physiologie).
MESH :

English descriptors

KwdEn :
- Adaptor Proteins, Signal Transducing (genetics), Adaptor Proteins, Signal Transducing (metabolism), Amino Acid Sequence (MeSH), Animals (MeSH), Bayes Theorem (MeSH), Databases, Genetic (MeSH), Drosophila Proteins (genetics), Drosophila Proteins (metabolism), Humans (MeSH), Interleukins (MeSH), Models, Molecular (MeSH), Myeloid Differentiation Factor 88 (genetics), Myeloid Differentiation Factor 88 (metabolism), Protein Domains (genetics), Protein Domains (physiology), Protein Structure, Secondary (MeSH), Receptors, Interleukin-1 (genetics), Receptors, Interleukin-1 (metabolism), Signal Transduction (genetics), Signal Transduction (physiology), Toll-Like Receptors (genetics), Toll-Like Receptors (metabolism).
MESH :
- chemical , genetics : Adaptor Proteins, Signal Transducing, Drosophila Proteins, Myeloid Differentiation Factor 88, Receptors, Interleukin-1, Toll-Like Receptors.
- chemical , metabolism : Adaptor Proteins, Signal Transducing, Drosophila Proteins, Myeloid Differentiation Factor 88, Receptors, Interleukin-1, Toll-Like Receptors.
- genetics : Protein Domains, Signal Transduction.
- physiology : Protein Domains, Signal Transduction.
- Amino Acid Sequence, Animals, Bayes Theorem, Databases, Genetic, Humans, Interleukins, Models, Molecular, Protein Structure, Secondary.

Abstract

Toll-interleukin-1R resistance (TIR) domains are ubiquitously present in all forms of cellular life. They are most commonly found in signaling proteins, as units responsible for signal-dependent formation of protein complexes that enable amplification and spatial propagation of the signal. A less common function of TIR domains is their ability to catalyze nicotinamide adenine dinucleotide degradation. This survey analyzes 26,414 TIR domains, automatically classified based on group-specific sequence patterns presumably determining biological function, using a statistical approach termed Bayesian partitioning with pattern selection (BPPS). We examine these groups and patterns in the light of available structures and biochemical analyses. Proteins within each of thirteen eukaryotic groups (10 metazoans and 3 plants) typically appear to perform similar functions, whereas proteins within each prokaryotic group typically exhibit diverse domain architectures, suggesting divergent functions. Groups are often uniquely characterized by structural fold variations associated with group-specific sequence patterns and by herein identified sequence motifs defining TIR domain functional divergence. For example, BPPS identifies, in helices C and D of TIRAP and MyD88 orthologs, conserved surface-exposed residues apparently responsible for specificity of TIR domain interactions. In addition, BPPS clarifies the functional significance of the previously described Box 2 and Box 3 motifs, each of which is a part of a larger, group-specific block of conserved, intramolecularly interacting residues.

DOI: 10.1007/s00251-020-01157-7
PubMed: 32002590
PubMed Central: PMC7075850

Affiliations:

États-Unis

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to stream Main, to step Corpus: 000232
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Le document en format XML

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<front><div type="abstract" xml:lang="en">Toll-interleukin-1R resistance (TIR) domains are ubiquitously present in all forms of cellular life. They are most commonly found in signaling proteins, as units responsible for signal-dependent formation of protein complexes that enable amplification and spatial propagation of the signal. A less common function of TIR domains is their ability to catalyze nicotinamide adenine dinucleotide degradation. This survey analyzes 26,414 TIR domains, automatically classified based on group-specific sequence patterns presumably determining biological function, using a statistical approach termed Bayesian partitioning with pattern selection (BPPS). We examine these groups and patterns in the light of available structures and biochemical analyses. Proteins within each of thirteen eukaryotic groups (10 metazoans and 3 plants) typically appear to perform similar functions, whereas proteins within each prokaryotic group typically exhibit diverse domain architectures, suggesting divergent functions. Groups are often uniquely characterized by structural fold variations associated with group-specific sequence patterns and by herein identified sequence motifs defining TIR domain functional divergence. For example, BPPS identifies, in helices C and D of TIRAP and MyD88 orthologs, conserved surface-exposed residues apparently responsible for specificity of TIR domain interactions. In addition, BPPS clarifies the functional significance of the previously described Box 2 and Box 3 motifs, each of which is a part of a larger, group-specific block of conserved, intramolecularly interacting residues.</div>
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	Serveur d'exploration sur les récepteurs immunitaires végétaux
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Serveur d'exploration sur les récepteurs immunitaires végétaux

A survey of TIR domain sequence and structure divergence.

A survey of TIR domain sequence and structure divergence.

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