1MHN

High resolution crystal structure of the SMN Tudor domain

1MHN の概要

• エントリーDOI: 10.2210/pdb1mhn/pdb
• 分子名称: Survival motor neuron protein (2 entities in total)
• 機能のキーワード: smn, sma, spinal muscular atrophy, rna binding protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm: Q16637
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 6649.45

構造登録者

Sprangers, R.,Groves, M.R.,Sinning, I.,Sattler, M. (登録日: 2002-08-20, 公開日: 2003-03-25, 最終更新日: 2024-02-14)

主引用文献

Sprangers, R.,Groves, M.R.,Sinning, I.,Sattler, M.
High Resolution X-ray and NMR Structures of the SMN Tudor Domain: conformational variation in the binding site for symmetrically dimethylated arginine residues
J.Mol.Biol., 327:507-520, 2003

PubMed Abstract: The SMN protein, which is linked to spinal muscular atrophy (SMA), plays an important role in the assembly of the spliceosomal small nuclear ribonucleoprotein complexes. This function requires binding of SMN to the arginine-glycine (RG) rich C-terminal tails of the Sm proteins, which contain symmetrically dimethylated arginine residues (sDMA) in vivo. Using NMR titrations, we show that the SMN Tudor domain recognizes these sDMAs in the methylated RG repeats. Upon complex formation a cluster of conserved aromatic residues in the SMN Tudor domain interacts with the sDMA methyl groups. We present two high resolution structures of the uncomplexed SMN Tudor domain, a 1.8A crystal structure and an NMR structure that has been refined against a large number of backbone and side-chain residual dipolar couplings. The backbone conformation of both structures is very similar, however, differences are observed for the cluster of conserved aromatic side-chains in the sDMA binding pocket. In order to validate these variations we introduce a novel application of residual dipolar couplings for aromatic rings. We show that structural information can be derived from aromatic ring residual dipolar couplings, even in the presence of internal motions such as ring flipping. These residual dipolar couplings and ring current shifts independently confirm that the SMN Tudor domain adopts two different conformations in the sDMA binding pocket. The observed structural variations may play a role for the recognition of sDMAs.

PubMed: 12628254
DOI: 10.1016/S0022-2836(03)00148-7

実験手法

X-RAY DIFFRACTION (1.8 Å)