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Publication Detail
Crystal structures of the human Dysferlin inner DysF domain.
  • Publication Type:
    Journal article
  • Publication Sub Type:
    Journal Article
  • Authors:
    Sula A, Cole AR, Yeats C, Orengo C, Keep NH
  • Publication date:
    17/01/2014
  • Pagination:
    3, ?
  • Journal:
    BMC Struct Biol
  • Volume:
    14
  • Status:
    Published online
  • Country:
    England
  • PII:
    1472-6807-14-3
  • Language:
    eng
  • Keywords:
    Arginine, Crystallography, X-Ray, Dysferlin, Humans, Hydrogen Bonding, Membrane Proteins, Models, Molecular, Muscle Proteins, Muscular Dystrophies, Limb-Girdle, Mutation, Missense, Protein Conformation, Protein Folding, Protein Structure, Secondary, Protein Structure, Tertiary, Sequence Alignment, Tryptophan
Abstract
BACKGROUND: Mutations in dysferlin, the first protein linked with the cell membrane repair mechanism, causes a group of muscular dystrophies called dysferlinopathies. Dysferlin is a type two-anchored membrane protein, with a single C terminal trans-membrane helix, and most of the protein lying in cytoplasm. Dysferlin contains several C2 domains and two DysF domains which are nested one inside the other. Many pathogenic point mutations fall in the DysF domain region. RESULTS: We describe the crystal structure of the human dysferlin inner DysF domain with a resolution of 1.9 Ã…ngstroms. Most of the pathogenic mutations are part of aromatic/arginine stacks that hold the domain in a folded conformation. The high resolution of the structure show that these interactions are a mixture of parallel ring/guanadinium stacking, perpendicular H bond stacking and aliphatic chain packing. CONCLUSIONS: The high resolution structure of the Dysferlin DysF domain gives a template on which to interpret in detail the pathogenic mutations that lead to disease.
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