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Solution structure of the inner DysF domain of myoferlin and implications for limb girdle muscular dystrophy type 2b. / Patel, Pryank; Harris, Richard; Geddes, Stella M.; Strehle, Eugen-Matthias; Watson, James D.; Bashir, Rumaisa; Bushby, Katharine; Driscoll, Paul C.; Keep, Nicholas H.

In: Journal of Molecular Biology, Vol. 379, No. 5, 20.06.2008, p. 981-90.

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Harvard

Patel, P, Harris, R, Geddes, SM, Strehle, E-M, Watson, JD, Bashir, R, Bushby, K, Driscoll, PC & Keep, NH 2008, 'Solution structure of the inner DysF domain of myoferlin and implications for limb girdle muscular dystrophy type 2b', Journal of Molecular Biology, vol. 379, no. 5, pp. 981-90. https://doi.org/10.1016/j.jmb.2008.04.046

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Vancouver

Author

Patel, Pryank ; Harris, Richard ; Geddes, Stella M. ; Strehle, Eugen-Matthias ; Watson, James D. ; Bashir, Rumaisa ; Bushby, Katharine ; Driscoll, Paul C. ; Keep, Nicholas H. / Solution structure of the inner DysF domain of myoferlin and implications for limb girdle muscular dystrophy type 2b. In: Journal of Molecular Biology. 2008 ; Vol. 379, No. 5. pp. 981-90.

Bibtex

@article{0338ee72b10b4ab79c135a54fa90109f,
title = "Solution structure of the inner DysF domain of myoferlin and implications for limb girdle muscular dystrophy type 2b",
abstract = "Mutations 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.",
keywords = "muscular dystrophy, dysferlin, myoferlin, Fer domain, NMR",
author = "Pryank Patel and Richard Harris and Geddes, {Stella M.} and Eugen-Matthias Strehle and Watson, {James D.} and Rumaisa Bashir and Katharine Bushby and Driscoll, {Paul C.} and Keep, {Nicholas H.}",
year = "2008",
month = "6",
day = "20",
doi = "10.1016/j.jmb.2008.04.046",
language = "English",
volume = "379",
pages = "981--90",
journal = "Journal of Molecular Biology",
issn = "0022-2836",
publisher = "Elsevier",
number = "5",

}

RIS

TY - JOUR

T1 - Solution structure of the inner DysF domain of myoferlin and implications for limb girdle muscular dystrophy type 2b

AU - Patel, Pryank

AU - Harris, Richard

AU - Geddes, Stella M.

AU - Strehle, Eugen-Matthias

AU - Watson, James D.

AU - Bashir, Rumaisa

AU - Bushby, Katharine

AU - Driscoll, Paul C.

AU - Keep, Nicholas H.

PY - 2008/6/20

Y1 - 2008/6/20

N2 - Mutations 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.

AB - Mutations 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.

KW - muscular dystrophy

KW - dysferlin

KW - myoferlin

KW - Fer domain

KW - NMR

U2 - 10.1016/j.jmb.2008.04.046

DO - 10.1016/j.jmb.2008.04.046

M3 - Article

C2 - 18495154

VL - 379

SP - 981

EP - 990

JO - Journal of Molecular Biology

JF - Journal of Molecular Biology

SN - 0022-2836

IS - 5

ER -