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Structure of filamin A immunoglobulin-like repeat 10 from Homo sapiens

Richard C Page1, Jeffrey G Clark, Saurav Misra

  • 1Department of Molecular Cardiology, Lerner Research Institute, Cleveland Clinic, Cleveland, OH 44195, USA. pager2@ccf.org

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications
|August 9, 2011
PubMed

Insights

Filamin A (FlnA) protein mutations in Ig10 domain cause otopalatodigital spectrum disorders. The crystal structure reveals how these mutations disrupt FlnA function, impacting cell structure and signaling pathways.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Genetics

Background:

  • Filamin A (FlnA) is crucial for cytoskeletal organization, cell motility, and signaling.
  • FlnA interacts with various proteins via its 24 immunoglobulin-like (Ig) domains.
  • Mutations in the FlnA Ig10 domain are linked to Melnick-Needles syndrome and frontometaphyseal dysplasia.

Purpose of the Study:

  • To elucidate the structural basis of FlnA mutations causing otopalatodigital spectrum disorders.
  • To understand how perturbations in the FlnA Ig10 domain affect protein function.

Main Methods:

  • X-ray crystallography was used to determine the structure of the FlnA Ig10 domain.
  • Analysis of the crystal structure at 2.44 Å resolution.

Main Results:

  • The crystal structure of FlnA-Ig10 was determined.
  • The structure provides insights into the molecular effects of disease-associated mutations.

Conclusions:

  • The structural data offers a molecular understanding of FlnA-Ig10 mutations.
  • This knowledge can aid in understanding the pathogenesis of related skeletal dysplasias.

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