Definition of domain boundaries and crystallization of the SMN Tudor domain

Remco Sprangers, Philipp Selenko, Michael Sattler, Irmgard Sinning, Matthew R. Groves

Research output: Contribution to journalArticlepeer-review

18 Scopus citations

Abstract

Spinal muscular atropy (SMA) is the major genetic disease leading to childhood mortality and is caused by mutations in or deletions of the smn1 gene. The human survival of motor neurons (SMN) protein encoded by this gene plays an important role in the assembly of snRNPs (small nuclear ribonucleoprotein complexes) via binding to the spliceosomal Sm proteins. The tails of these Sm proteins contain symmetrically dimethylated arginines that are recognized by the central SMN Tudor domain. To gain insight in the molecular basis of this specific interaction, the SMN Tudor domain has been crystallized. The rapid crystallization of the protein and the high stability of the crystals is facilitated by redefinition of domain boundaries based on NMR relaxation experiments and the previously determined solution structure. The crystals diffract to high resolution (1.8 Å) and a complete data set has been collected from a hexagonal crystal form (P61/P65), with unit-cell parameters a = b = 27.65, c = 110.30 Å, α = • = 90, γ = 120°. Crystal soaks and co-crystallization with peptides derived from the Sm protein tails have been initiated. Molecular replacement with the NMR coordinates is under way.

Original languageEnglish
Pages (from-to)366-368
Number of pages3
JournalActa Crystallographica Section D: Biological Crystallography
Volume59
Issue number2
DOIs
StatePublished - 1 Feb 2003
Externally publishedYes

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