Article
Molecular basis of filamin A-FilGAP interaction and its impairment in congenital disorders associated with filamin A mutations.
PloS one - 1 Jan 2009
Nakamura Fumihiko, Heikkinen Outi, Pentikäinen Olli T, Osborn Teresia M, Kasza Karen E, Weitz David A, Kupiainen Olga, Permi Perttu, Kilpeläinen Ilkka, Ylänne Jari, Hartwig John H, Stossel Thomas P
Abstract excerpt
BACKGROUND: Mutations in filamin A (FLNa), an essential cytoskeletal protein with multiple binding partners, cause developmental anomalies in humans. METHODOLOGY/PRINCIPAL FINDINGS: We determined the structure of the 23rd Ig repeat of FLNa (IgFLNa23) that interacts with FilGAP, a Rac-specific GTPase-activating protein and regulator of cell polarity and movement, and the effect of the three disease-related...
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