2k2o
Solution Structure of the inner DysF domain of human myoferlinSolution Structure of the inner DysF domain of human myoferlin
Structural highlights
Function[MYOF_HUMAN] Calcium/phospholipid-binding protein that plays a role in the plasmalemma repair mechanism of endothelial cells that permits rapid resealing of membranes disrupted by mechanical stress. Involved in endocytic recycling. Implicated in VEGF signal transduction by regulating the levels of the receptor KDR (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedMutations in the protein dysferlin, a member of the ferlin family, lead to limb girdle muscular dystrophy type 2B and Myoshi myopathy. The ferlins are large proteins characterised by multiple C2 domains and a single C-terminal membrane-spanning helix. However, there is sequence conservation in some of the ferlin family in regions outside the C2 domains. In one annotation of the domain structure of these proteins, an unusual internal duplication event has been noted where a putative domain is inserted in between the N- and C-terminal parts of a homologous domain. This domain is known as the DysF domain. Here, we present the solution structure of the inner DysF domain of the dysferlin paralogue myoferlin, which has a unique fold held together by stacking of arginine and tryptophans, mutations that lead to clinical disease in dysferlin. Solution structure of the inner DysF domain of myoferlin and implications for limb girdle muscular dystrophy type 2b.,Patel P, Harris R, Geddes SM, Strehle EM, Watson JD, Bashir R, Bushby K, Driscoll PC, Keep NH J Mol Biol. 2008 Jun 20;379(5):981-90. Epub 2008 Apr 26. PMID:18495154[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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