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2N34

NMR assignments and solution structure of the JAK interaction region of SOCS5

2MP6」から置き換えられました
2N34 の概要
エントリーDOI10.2210/pdb2n34/pdb
NMR情報BMRB: 19966
分子名称Suppressor of cytokine signaling 5 (1 entity in total)
機能のキーワードsuppressor of cytokine signalling, jak interaction region, intrinsically unstructured protein, signaling protein
由来する生物種Mus musculus (mouse)
タンパク質・核酸の鎖数1
化学式量合計8116.52
構造登録者
Chandrashekaran, I.R.,Mohanty, B.,Linossi, E.M.,Nicholson, S.E.,Babon, J.,Norton, R.S.,Dagley, L.F.,Leung, E.W.W.,Murphy, J.M. (登録日: 2015-05-21, 公開日: 2015-07-29, 最終更新日: 2024-05-15)
主引用文献Chandrashekaran, I.R.,Mohanty, B.,Linossi, E.M.,Dagley, L.F.,Leung, E.W.,Murphy, J.M.,Babon, J.J.,Nicholson, S.E.,Norton, R.S.
Structure and Functional Characterization of the Conserved JAK Interaction Region in the Intrinsically Disordered N-Terminus of SOCS5.
Biochemistry, 54:4672-4682, 2015
Cited by
PubMed Abstract: SOCS5 can negatively regulate both JAK/STAT and EGF-receptor pathways and has therefore been implicated in regulating both the immune response and tumorigenesis. Understanding the molecular basis for SOCS5 activity may reveal novel ways to target key components of these signaling pathways. The N-terminal region of SOCS5 coordinates critical protein interactions involved in inhibition of JAK/STAT signaling, and a conserved region within the N-terminus of SOCS5 mediates direct binding to the JAK kinase domain. Here we have characterized the solution conformation of this conserved JAK interaction region (JIR) within the largely disordered N-terminus of SOCS5. Using nuclear magnetic resonance (NMR) chemical shift analysis, relaxation measurements, and NOE analysis, we demonstrate the presence of preformed structural elements in the JIR of mouse SOCS5 (mSOCS5175-244), consisting of an α-helix encompassing residues 224-233, preceded by a turn and an extended structure. We have identified a phosphorylation site (Ser211) within the JIR of mSOCS5 and have investigated the role of phosphorylation in modulating JAK binding using site-directed mutagenesis.
PubMed: 26173083
DOI: 10.1021/acs.biochem.5b00619
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 2n34
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2025-07-16に公開中

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