6F7M

NMR structure of EphA2-Sam stapled peptides (S13ST)

6F7M の概要

• エントリーDOI: 10.2210/pdb6f7m/pdb
• 関連するPDBエントリー: 6F7N 6F7O
• NMR情報: BMRB: 34213
• 分子名称: Ephrin type-A receptor 2 (1 entity in total)
• 機能のキーワード: ephrin receptor, sam domain, stapled peptide, signaling protein
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 2905.53

構造登録者

Mercurio, F.A.,Leone, M. (登録日: 2017-12-11, 公開日: 2018-08-01, 最終更新日: 2024-11-13)

主引用文献

Mercurio, F.A.,Pirone, L.,Di Natale, C.,Marasco, D.,Pedone, E.M.,Leone, M.
Sam domain-based stapled peptides: Structural analysis and interaction studies with the Sam domains from the EphA2 receptor and the lipid phosphatase Ship2.
Bioorg. Chem., 80:602-610, 2018

PubMed Abstract: Sam (Sterile alpha motif) domains represent small helical protein-protein interaction modules which play versatile functions in different cellular processes. The Sam domain from the EphA2 receptor binds the Sam domain of the lipid phosphatase Ship2 and this interaction modulates receptor endocytosis and degradation primarily generating pro-oncogenic effects in cell. To identify molecule antagonists of the EphA2-Sam/Ship2-Sam complex with anti-cancer activity, we focused on hydrocarbon helical stapled peptides. EphA2-Sam and one of its interactors (i.e., the first Sam domain of the adaptor protein Odin) were used as model systems for peptide design. Increase in helicity in the stapled peptides, with respect to the corresponding linear/native-like regions, was proved by structural studies conducted through CD (Circular Dichroism) and NMR (Nuclear Magnetic Resonance). Interestingly, interaction assays by means of NMR, SPR (Surface Plasmon Resonance) and MST (MicroScale Thermophoresis) techniques led to the discovery of a novel ligand of Ship2-Sam.

PubMed: 30036816
DOI: 10.1016/j.bioorg.2018.07.013

実験手法

SOLUTION NMR