Crystal structures of the human Dysferlin inner DysF domain View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2014-12

AUTHORS

Altin Sula, Ambrose R Cole, Corin Yeats, Christine Orengo, Nicholas H Keep

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 Ångstroms. 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. More... »

PAGES

3

Identifiers

URI

http://scigraph.springernature.com/pub.10.1186/1472-6807-14-3

DOI

http://dx.doi.org/10.1186/1472-6807-14-3

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1026196932

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/24438169


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