1YA0

Crystal structure of the N-terminal domain of human SMG7

1YA0 の概要

• エントリーDOI: 10.2210/pdb1ya0/pdb
• 分子名称: SMG-7 transcript variant 2, SULFATE ION (3 entities in total)
• 機能のキーワード: alpha-helical repeat, tetratricopetide repeat (tpr), 14-3-3, signaling protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm: Q92540
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 114627.97

構造登録者

Fukuhara, N.,Ebert, J.,Unterholzner, L.,Lindner, D.,Izaurralde, E.,Conti, E. (登録日: 2004-12-17, 公開日: 2005-03-15, 最終更新日: 2024-02-14)

主引用文献

Fukuhara, N.,Ebert, J.,Unterholzner, L.,Lindner, D.,Izaurralde, E.,Conti, E.
SMG7 Is a 14-3-3-like Adaptor in the Nonsense-Mediated mRNA Decay Pathway.
Mol.Cell, 17:537-547, 2005

PubMed Abstract: In metazoa, regulation of the phosphorylation state of UPF1 is crucial for nonsense-mediated mRNA decay (NMD), a process by which aberrant mRNAs containing nonsense mutations are degraded. UPF1 is targeted for dephosphorylation by three related proteins, SMG5, SMG6, and SMG7. We report here the crystal structure of the N-terminal domain of SMG7. The structure reveals that SMG7 contains a 14-3-3-like domain. Residues that bind phosphoserine-containing peptides in 14-3-3 are conserved at the equivalent positions in SMG7. Mutation of these residues impairs UPF1 binding to SMG7 in vitro and UPF1 recruitment to cytoplasmic mRNA decay foci in vivo, suggesting that SMG7 acts as an adaptor in targeting mRNAs associated with phosphorylated UPF1 for degradation. The 14-3-3 site of SMG7 is conserved in SMG5 and SMG6. These data also imply that the homologous human Est1 might have a 14-3-3 function at telomeres, and that phosphorylation events may be important for telomerase regulation.

PubMed: 15721257
DOI: 10.1016/j.molcel.2005.01.010

実験手法

X-RAY DIFFRACTION (2.55 Å)