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Article

The structure of the CYLD USP domain explains its specificity for Lys63-linked polyubiquitin and reveals a B box module.

Molecular cell - 29 Feb 2008

Komander David, Lord Christopher J, Scheel Hartmut, Swift Sally, Hofmann Kay, Ashworth Alan, Barford David

Abstract excerpt

The tumor suppressor CYLD antagonizes NF-kappaB and JNK signaling by disassembly of Lys63-linked ubiquitin chains synthesized in response to cytokine stimulation. Here we describe the crystal structure of the CYLD USP domain, revealing a distinctive architecture that provides molecular insights into its specificity toward Lys63-linked polyubiquitin. We identify regions of the USP domain responsible for this...

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Share to Deubiquitinating Enzyme CYLD
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to JNK Mitogen-Activated Protein Kinases

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Source

Identifiers

PMID: 18313383
DOI: 10.1016/j.molcel.2007.12.018

Genes

CYLD

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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The structure of the CYLD USP domain explains its specificity for Lys63-linked polyubiquitin and reveals a B box module.PMID 18313383Read ↗

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