3MX0
Crystal Structure of EphA2 ectodomain in complex with ephrin-A5
3MX0 の概要
エントリーDOI | 10.2210/pdb3mx0/pdb |
関連するBIRD辞書のPRD_ID | PRD_900017 |
分子名称 | Ephrin type-A receptor 2, Ephrin-A5, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total) |
機能のキーワード | ectodomain, receptor-ligand complex, receptor-receptor interaction, transferase receptor-signalling protein complex, transferase receptor/signalling protein |
由来する生物種 | Homo sapiens (human) 詳細 |
タンパク質・核酸の鎖数 | 4 |
化学式量合計 | 124331.22 |
構造登録者 | 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. (登録日: 2010-05-06, 公開日: 2010-06-30, 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 Cited by 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: 20505120DOI: 10.1073/pnas.1004148107 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (3.506 Å) |
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