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

Journal of Molecular Biology

Volumn 327, Issue 2, 2003, Pages 507-520

  Sprangers, Remco ^a   Groves, Matthew R ^b   Sinning, Irmgard ^b   Sattler, Michael ^a  

^a EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

^b UNIVERSITY OF HEIDELBERG   (Germany)

Author keywords

NMR and X ray structure comparison; Residual dipolar couplings (RDCs); SMN Tudor domain; Spinal muscular atrophy (SMA); Symmetrically dimethylated arginine (sDMA)

Indexed keywords

ARGININE; CELL PROTEIN; SURVIVAL MOTOR NEURON PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; BINDING SITE; CARBOXY TERMINAL SEQUENCE; CRYSTAL STRUCTURE; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN STRUCTURE; X RAY ANALYSIS;

EID: 0037459239     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(03)00148-7     Document Type: Article

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