3C8X

Crystal structure of the ligand binding domain of human Ephrin A2 (Epha2) receptor protein kinase

3C8X の概要

• エントリーDOI: 10.2210/pdb3c8x/pdb
• 関連するPDBエントリー: 1MQB
• 分子名称: Ephrin type-A receptor 2 (2 entities in total)
• 機能のキーワード: atp-binding, kinase, nucleotide-binding, receptor, transferase, phosphorylation, transmembrane, tyrosine-protein kinase, glycoprotein, structural genomics consortium, sgc, phosphoprotein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cell membrane ; Single-pass type I membrane protein : P29317
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 23568.52

構造登録者

Walker, J.R.,Yermekbayeva, L.,Seitova, A.,Butler-Cole, C.,Bountra, C.,Weigelt, J.,Arrowsmith, C.H.,Edwards, A.M.,Bochkarev, A.,Dhe-Paganon, S.,Structural Genomics Consortium (SGC) (登録日: 2008-02-14, 公開日: 2008-03-25, 最終更新日: 2024-10-30)

主引用文献

Himanen, J.P.,Yermekbayeva, L.,Janes, P.W.,Walker, J.R.,Xu, K.,Atapattu, L.,Rajashankar, K.R.,Mensinga, A.,Lackmann, M.,Nikolov, D.B.,Dhe-Paganon, S.
Architecture of Eph receptor clusters.
Proc.Natl.Acad.Sci.USA, 107:10860-10865, 2010

PubMed Abstract: Eph receptor tyrosine kinases and their ephrin ligands regulate cell navigation during normal and oncogenic development. Signaling of Ephs is initiated in a multistep process leading to the assembly of higher-order signaling clusters that set off bidirectional signaling in interacting cells. However, the structural and mechanistic details of this assembly remained undefined. Here we present high-resolution structures of the complete EphA2 ectodomain and complexes with ephrin-A1 and A5 as the base unit of an Eph cluster. The structures reveal an elongated architecture with novel Eph/Eph interactions, both within and outside of the Eph ligand-binding domain, that suggest the molecular mechanism underlying Eph/ephrin clustering. Structure-function analysis, by using site-directed mutagenesis and cell-based signaling assays, confirms the importance of the identified oligomerization interfaces for Eph clustering.

PubMed: 20505120
DOI: 10.1073/pnas.1004148107

実験手法

X-RAY DIFFRACTION (1.95 Å)