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2LXA

Solution structure of the Get5 ubiquitin-like domain

2LXA の概要
エントリーDOI10.2210/pdb2lxa/pdb
関連するPDBエントリー2LXB 2LXC 4GOC 4GOD 4GOE 4GOF
NMR情報BMRB: 18669
分子名称Ubiquitin-like protein MDY2 (1 entity in total)
機能のキーワードubiquitin-like domain, protein-protein interaction, sgt2 binding domain, get pathway, protein binding
由来する生物種Saccharomyces cerevisiae (Baker's yeast)
細胞内の位置Cytoplasm, cytosol: Q12285
タンパク質・核酸の鎖数1
化学式量合計9999.68
構造登録者
Chartron, J.W.,Vandervelde, D.G.,Clemons Jr., W.M. (登録日: 2012-08-19, 公開日: 2012-11-21, 最終更新日: 2024-05-15)
主引用文献Chartron, J.W.,Vandervelde, D.G.,Clemons, W.M.
Structures of the Sgt2/SGTA Dimerization Domain with the Get5/UBL4A UBL Domain Reveal an Interaction that Forms a Conserved Dynamic Interface.
Cell Rep, 2:1620-1632, 2012
Cited by
PubMed Abstract: In the cytoplasm, the correct delivery of membrane proteins is an essential and highly regulated process. The posttranslational targeting of the important tail-anchor membrane (TA) proteins has recently been under intense investigation. A specialized pathway, called the guided entry of TA proteins (GET) pathway in yeast and the transmembrane domain recognition complex (TRC) pathway in vertebrates, recognizes endoplasmic-reticulum-targeted TA proteins and delivers them through a complex series of handoffs. An early step is the formation of a complex between Sgt2/SGTA, a cochaperone with a presumed ubiquitin-like-binding domain (UBD), and Get5/UBL4A, a ubiquitin-like domain (UBL)-containing protein. We structurally characterize this UBD/UBL interaction for both yeast and human proteins. This characterization is supported by biophysical studies that demonstrate that complex formation is mediated by electrostatics, generating an interface that has high-affinity with rapid kinetics. In total, this work provides a refined model of the interplay of Sgt2 homologs in TA targeting.
PubMed: 23142665
DOI: 10.1016/j.celrep.2012.10.010
主引用文献が同じPDBエントリー
実験手法
SOLUTION NMR
構造検証レポート
Validation report summary of 2lxa
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-02-04に公開中

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