1K2F

siah, Seven In Absentia Homolog

1K2F の概要

• エントリーDOI: 10.2210/pdb1k2f/pdb
• 分子名称: siah-1A protein, ZINC ION, BETA-MERCAPTOETHANOL, ... (4 entities in total)
• 機能のキーワード: beta-sandwich, ligase, protein binding
• 由来する生物種: Mus musculus (house mouse)
• 細胞内の位置: Cytoplasm: P61092
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 43552.05

構造登録者

Polekhina, G.,House, C.M.,Traficante, N.,Mackay, J.P.,Relaix, F.,Sassoon, D.A.,Parker, M.W.,Bowtell, D.D.L. (登録日: 2001-09-26, 公開日: 2001-12-28, 最終更新日: 2025-03-26)

主引用文献

Polekhina, G.,House, C.M.,Traficante, N.,Mackay, J.P.,Relaix, F.,Sassoon, D.A.,Parker, M.W.,Bowtell, D.D.
Siah ubiquitin ligase is structurally related to TRAF and modulates TNF-alpha signaling.
Nat.Struct.Biol., 9:68-75, 2002

PubMed Abstract: Members of the Siah (seven in absentia homolog) family of RING domain proteins are components of E3 ubiquitin ligase complexes that catalyze ubiquitination of proteins. We have determined the crystal structure of the substrate-binding domain (SBD) of murine Siah1a to 2.6 A resolution. The structure reveals that Siah is a dimeric protein and that the SBD adopts an eight-stranded beta-sandwich fold that is highly similar to the TRAF-C region of TRAF (TNF-receptor associated factor) proteins. The TRAF-C region interacts with TNF-alpha receptors and TNF-receptor associated death-domain (TRADD) proteins; however, our findings indicate that these interactions are unlikely to be mimicked by Siah. The Siah structure also reveals two novel zinc fingers in a region with sequence similarity to TRAF. We find that the Siah1a SBD potentiates TNF-alpha-mediated NF-kappa B activation. Therefore, Siah proteins share important similarities with the TRAF family of proteins, including their overall domain architecture, three-dimensional structure and functional activity.

PubMed: 11742346
DOI: 10.1038/nsb743

実験手法

X-RAY DIFFRACTION (2.6 Å)