Crystal Structures of a Formin Homology-2 Domain Reveal a Tethered Dimer Architecture

@article{Xu2004CrystalSO,
  title={Crystal Structures of a Formin Homology-2 Domain Reveal a Tethered Dimer Architecture},
  author={Yingwu Xu and James B Moseley and Isabelle Sagot and Florence Poy and David S Pellman and Bruce L. Goode and Michael J. Eck},
  journal={Cell},
  year={2004},
  volume={116},
  pages={711-723}
}
Formin proteins participate in a wide range of cytoskeletal processes in all eukaryotes. The defining feature of formins is a highly conserved approximately 400 residue region, the Formin Homology-2 (FH2) domain, which has recently been found to nucleate actin filaments. Here we report crystal structures of the S. cerevesiae Bni1p FH2 domain. The mostly alpha-helical FH2 domain forms a unique "tethered dimer" in which two elongated actin binding heads are tied together at either end by an… CONTINUE READING
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