1G5V

SOLUTION STRUCTURE OF THE TUDOR DOMAIN OF THE HUMAN SMN PROTEIN

1G5V の概要

• エントリーDOI: 10.2210/pdb1g5v/pdb
• NMR情報: BMRB: 4899
• 分子名称: SURVIVAL MOTOR NEURON PROTEIN 1 (1 entity in total)
• 機能のキーワード: mrna processing, translation
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9796.64

構造登録者

Selenko, P.,Sprangers, R.,Stier, G.,Buehler, D.,Fischer, U.,Sattler, M. (登録日: 2000-11-02, 公開日: 2001-05-02, 最終更新日: 2024-05-01)

主引用文献

Selenko, P.,Sprangers, R.,Stier, G.,Buhler, D.,Fischer, U.,Sattler, M.
SMN tudor domain structure and its interaction with the Sm proteins.
Nat.Struct.Biol., 8:27-31, 2001

PubMed Abstract: Spinal muscular atrophy (SMA) is a common motor neuron disease that results from mutations in the Survival of Motor Neuron (SMN) gene. The SMN protein plays a crucial role in the assembly of spliceosomal uridine-rich small nuclear ribonucleoprotein (U snRNP) complexes via binding to the spliceosomal Sm core proteins. SMN contains a central Tudor domain that facilitates the SMN-Sm protein interaction. A SMA-causing point mutation (E134K) within the SMN Tudor domain prevents Sm binding. Here, we have determined the three-dimensional structure of the Tudor domain of human SMN. The structure exhibits a conserved negatively charged surface that is shown to interact with the C-terminal Arg and Gly-rich tails of Sm proteins. The E134K mutation does not disrupt the Tudor structure but affects the charge distribution within this binding site. An intriguing structural similarity between the Tudor domain and the Sm proteins suggests the presence of an additional binding interface that resembles that in hetero-oligomeric complexes of Sm proteins. Our data provide a structural basis for a molecular defect underlying SMA.

PubMed: 11135666
DOI: 10.1038/83014

実験手法

SOLUTION NMR