(Q27640685)

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High-resolution X-ray and NMR structures of the SMN Tudor domain: conformational variation in the binding site for symmetrically dimethylated arginine residues

scientific article (publication date: 21 March 2003)

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scholarly article

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High-resolution X-ray and NMR structures of the SMN Tudor domain: conformational variation in the binding site for symmetrically dimethylated arginine residues (English)

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Michael Sattler

4

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Irmgard Sinning

3

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Matthew R Groves

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Matthew R Groves

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author name string

Remco Sprangers

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language of work or name

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publication date

21 March 2003

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Journal of Molecular Biology

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327

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2

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507-20

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Spinal muscular atrophy

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SMN tudor domain structure and its interaction with the Sm proteins

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The C-terminal RG dipeptide repeats of the spliceosomal Sm proteins D1 and D3 contain symmetrical dimethylarginines, which form a major B-cell epitope for anti-Sm autoantibodies

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Symmetrical dimethylation of arginine residues in spliceosomal Sm protein B/B' and the Sm-like protein LSm4, and their interaction with the SMN protein.

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SMN, the product of the spinal muscular atrophy gene, binds preferentially to dimethylarginine-containing protein targets

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10.1016/S0022-2836(03)00148-7

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