3CZU
Crystal structure of the human ephrin A2- ephrin A1 complex
Summary for 3CZU
| Entry DOI | 10.2210/pdb3czu/pdb |
| Related | 1MQB 3C8X |
| Descriptor | Ephrin type-A receptor 2, Ephrin-A1, alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total) |
| Functional Keywords | atp-binding, kinase, nucleotide-binding, receptor, transferase, phosphorylation, transmembrane, tyrosine-protein kinase, glycoprotein, structural genomics consortium, sgc, phosphoprotein, gpi-anchor, lipoprotein, transferase-signaling protein complex, transferase/signaling protein |
| Biological source | Homo sapiens More |
| Cellular location | Cell membrane; Single-pass type I membrane protein: P29317 Cell membrane; Lipid-anchor, GPI-anchor. Ephrin-A1, secreted form: Secreted: P20827 |
| Total number of polymer chains | 2 |
| Total formula weight | 45695.90 |
| Authors | Walker, J.R.,Yermekbayeva, L.,Seitova, A.,Butler-Cole, C.,Bountra, C.,Wikstrom, M.,Arrowsmith, C.H.,Edwards, A.M.,Bochkarev, A.,Dhe-Paganon, S.,Structural Genomics Consortium (SGC) (deposition date: 2008-04-30, release date: 2008-08-12, Last modification date: 2023-08-30) |
| Primary citation | 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 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.65 Å) |
Structure validation
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