Key result
The crystal structure of human DAAM1 FH2 dimer at 2.8 A resolution reveals a highly flexible dimer architecture, with the N-terminal linker length being crucial for actin assembly activity.
Population
Human DAAM1 FH2 domain
Comparison
X-ray crystallography and actin assembly assays… vs Mouse mDia1 and yeast Bni1p structures
Design
Preclinical
Authors
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No immediate clinical impact; extends formin biology by revealing flexible mammalian DAAM1 dimer architecture.
This study provides the first dimeric structure of a mammalian formin, highlighting the flexibility of the dimer architecture in the actin-free state.
Yamashita et al. (2007) studied this question. The crystal structure of human DAAM1 FH2 dimer at 2.8 A resolution reveals a highly flexible dimer architecture, with the N-terminal linker length being crucial for actin assembly activity.
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