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Article

Structure of the FH2 domain of Daam1: implications for formin regulation of actin assembly.

Journal of molecular biology - 22 Jun 2007

Lu Jun, Meng Wuyi, Poy Florence, Maiti Sankar, Goode Bruce L, Eck Michael J

Abstract excerpt

Daam1 (dishevelled-associated activator of morphogenesis-1) is a diaphanous-related formin first studied as a novel dishevelled binding protein and shown to be crucial for the planar cell polarity (PCP) pathway in Xenopus. Daam1, like other formins, directs nucleation and elongation of new actin filaments using its conserved formin-homology-2 (FH2) domain. Here we report the crystal structure of a large...

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Identifiers

PMID: 17482208
DOI: 10.1016/j.jmb.2007.04.002
PMCID: PMC1939941

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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