4DKK

The X-ray Crystal Structure of the Human STAU1 SSM-'RBD'5 Domain-Swapped Dimer

4DKK の概要

• エントリーDOI: 10.2210/pdb4dkk/pdb
• 分子名称: Double-stranded RNA-binding protein Staufen homolog 1, CITRATE ANION, CHLORIDE ION, ... (4 entities in total)
• 機能のキーワード: rbd, beta sheet, swapping-motif, dimerization, protein binding, rna binding protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm: O95793
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12700.69

構造登録者

Gleghorn, M.L. (登録日: 2012-02-03, 公開日: 2013-03-20, 最終更新日: 2024-03-13)

主引用文献

Gleghorn, M.L.,Gong, C.,Kielkopf, C.L.,Maquat, L.E.
Staufen1 dimerizes through a conserved motif and a degenerate dsRNA-binding domain to promote mRNA decay.
Nat.Struct.Mol.Biol., 20:515-524, 2013

PubMed Abstract: Staufen1 (STAU1)-mediated mRNA decay (SMD) degrades mammalian-cell mRNAs that bind the double-stranded RNA (dsRNA)-binding protein STAU1 in their 3' untranslated region. We report a new motif, which typifies STAU homologs from all vertebrate classes, that is responsible for human STAU1 (hSTAU1) homodimerization. Our crystal structure and mutagenesis analyses reveal that this motif, which we named the Staufen-swapping motif (SSM), and the dsRNA-binding domain 5 ('RBD'5) mediate protein dimerization: the two SSM α-helices of one molecule interact primarily through a hydrophobic patch with the two 'RBD'5 α-helices of a second molecule. 'RBD'5 adopts the canonical α-β-β-β-α fold of a functional RBD, but it lacks residues and features required to bind duplex RNA. In cells, SSM-mediated hSTAU1 dimerization increases the efficiency of SMD by augmenting hSTAU1 binding to the ATP-dependent RNA helicase hUPF1. Dimerization regulates keratinocyte-mediated wound healing and many other cellular processes.

PubMed: 23524536
DOI: 10.1038/nsmb.2528

実験手法

X-RAY DIFFRACTION (1.701 Å)