4CA1

Crystal structure of Siah1 at 1.58 A resolution.

4CA1 の概要

• エントリーDOI: 10.2210/pdb4ca1/pdb
• 関連するPDBエントリー: 4C9Z
• 分子名称: E3 UBIQUITIN-PROTEIN LIGASE SIAH1, ZINC ION, SULFATE ION, ... (6 entities in total)
• 機能のキーワード: ligase
• 由来する生物種: HOMO SAPIENS (HUMAN)
• 細胞内の位置: Cytoplasm: Q8IUQ4
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 45795.60

構造登録者

Rimsa, V.,Eadsforth, T.C.,Hunter, W.N. (登録日: 2013-10-04, 公開日: 2013-10-16, 最終更新日: 2023-12-20)

主引用文献

Rimsa, V.,Eadsforth, T.C.,Hunter, W.N.
Two High-Resolution Structures of the Human E3 Ubiquitin Ligase Siah1.
Acta Crystallogr.,Sect.F, 96:1339-, 2013

PubMed Abstract: Siah1 is an E3 ubiquitin ligase that contributes to proteasome-mediated degradation of multiple targets in key cellular processes and which shows promise as a therapeutic target in oncology. Structures of a truncated Siah1 bound to peptide-based inhibitors have been reported. Here, new crystallization conditions have allowed the determination of a construct encompassing dual zinc-finger subdomains and substrate-binding domains at significantly higher resolution. Although the crystals appear isomorphous, two structures present distinct states in which the spatial orientation of one zinc-finger subdomain differs with respect to the rest of the dimeric protein. Such a difference, which is indicative of conformational freedom, infers potential biological relevance related to recognition of binding partners. The crystallization conditions and improved models of Siah1 may aid future studies investigating Siah1-ligand complexes.

PubMed: 24316825
DOI: 10.1107/S1744309113031448

実験手法

X-RAY DIFFRACTION (1.58 Å)