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Article

Disorder in a target for the smad2 mad homology 2 domain and its implications for binding and specificity.

The Journal of biological chemistry - 24 Sept 2004

Chong P Andrew, Ozdamar Barish, Wrana Jeffrey L, Forman-Kay Julie D

Abstract excerpt

The Smad2 Mad homology 2 (MH2) domain binds to a diverse group of proteins which do not share a common sequence motif. We have used NMR to investigate the structure of one of these interacting proteins, the Smad binding domain (SBD) of Smad anchor for receptor activation (SARA). Our results indicate that the unbound SBD is highly disordered and forms no stable secondary or tertiary structures. Additionally we...

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Identifiers

PMID: 15231848
DOI: 10.1074/jbc.M404375200

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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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