Structural and functional characterization of human Iba proteins.

@article{Schulze2008StructuralAF,
  title={Structural and functional characterization of human Iba proteins.},
  author={J{\"o}rg O. Schulze and Claudia Quedenau and Yvette Roske and Thomas Adam and Herwig Sch{\"u}ler and Joachim Behlke and Andrew P. Turnbull and Volker Sievert and Christoph M. A. Scheich and Uwe Mueller and Udo Heinemann and Konrad B{\"u}ssow},
  journal={The FEBS journal},
  year={2008},
  volume={275 18},
  pages={
          4627-40
        }
}
Iba2 is a homolog of ionized calcium-binding adapter molecule 1 (Iba1), a 17-kDa protein that binds and cross-links filamentous actin (F-actin) and localizes to membrane ruffles and phagocytic cups. Here, we present the crystal structure of human Iba2 and its homodimerization properties, F-actin cross-linking activity, cellular localization and recruitment upon bacterial invasion in comparison with Iba1. The Iba2 structure comprises two central EF-hand motifs lacking bound Ca2+. Iba2… CONTINUE READING

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