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Article

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 - 1 Feb 2015

Huber Roland G, Eibl Clarissa, Fuchs Julian E

Abstract excerpt

Nucleotide-binding domain leucine-rich repeat-containing receptors (NLRs) are key proteins in the innate immune system. The 14 members of the NLRP family of NLRs contain an N-terminal pyrin domain which is central for complex formation and signal transduction. Recently, X-ray structures of NLRP14...

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Topics

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Share to Adaptor Proteins, Signal Transducing
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Share to Protein Folding

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Share to Protein Structure, Tertiary

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Source

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Identifiers

PMID: 25403012
DOI: 10.1002/pro.2601
PMCID: PMC4315655

Genes

NLRP14
NLRP4

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-25403012-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

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