2K2O

Solution Structure of the inner DysF domain of human myoferlin

Summary for 2K2O

• Entry DOI: 10.2210/pdb2k2o/pdb
• NMR Information: BMRB: 15718
• Descriptor: Myoferlin (1 entity in total)
• Functional Keywords: myoferlin, muscular dystrophy, dysf, dysferlin, limb-girdle, alternative splicing, membrane, nucleus, phosphoprotein, polymorphism, transmembrane, membrane protein
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 1
• Total formula weight: 14195.44

Authors

Patel, P.,Harris, R.,Keep, N.,Driscoll, P. (deposition date: 2008-04-07, release date: 2008-06-10, Last modification date: 2024-05-01)

Primary citation

Patel, P.,Harris, R.,Geddes, S.M.,Strehle, E.M.,Watson, J.D.,Bashir, R.,Bushby, K.,Driscoll, P.C.,Keep, N.H.
Solution structure of the inner DysF domain of myoferlin and implications for limb girdle muscular dystrophy type 2b.
J.Mol.Biol., 379:981-990, 2008

PubMed 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.

PubMed: 18495154
DOI: 10.1016/j.jmb.2008.04.046

Experimental method

SOLUTION NMR