Entry Database : PDB / ID : 2wo1 Structure visualization Downloads & linksTitle Crystal Structure of the EphA4 Ligand Binding Domain ComponentsEPHRIN TYPE-A RECEPTOR Details Keywords TRANSFERASE / GLYCOPROTEIN / AXON GUIDANCE / VASCULAR DEVELOPMENT / CELL SURFACE RECEPTOR / CELL SIGNALINGFunction / homology Function and homology informationFunction Domain/homology Component
DH domain binding / neuron projection fasciculation / regulation of astrocyte differentiation / negative regulation of proteolysis involved in protein catabolic process / corticospinal tract morphogenesis / positive regulation of Rho guanyl-nucleotide exchange factor activity / neuron projection guidance / PH domain binding / nephric duct morphogenesis / negative regulation of cellular response to hypoxia ... DH domain binding / neuron projection fasciculation / regulation of astrocyte differentiation / negative regulation of proteolysis involved in protein catabolic process / corticospinal tract morphogenesis / positive regulation of Rho guanyl-nucleotide exchange factor activity / neuron projection guidance / PH domain binding / nephric duct morphogenesis / negative regulation of cellular response to hypoxia / fasciculation of motor neuron axon / fasciculation of sensory neuron axon / synapse pruning / glial cell migration / negative regulation of axon regeneration / GPI-linked ephrin receptor activity / regulation of modification of synaptic structure / regulation of dendritic spine morphogenesis / negative regulation of epithelial to mesenchymal transition / transmembrane-ephrin receptor activity / adult walking behavior / negative regulation of cell adhesion / motor neuron axon guidance / positive regulation of dendrite morphogenesis / positive regulation of aspartic-type endopeptidase activity involved in amyloid precursor protein catabolic process / adherens junction organization / EPH-Ephrin signaling / cochlea development / EPHA-mediated growth cone collapse / regulation of axonogenesis / positive regulation of amyloid-beta formation / axon terminus / negative regulation of long-term synaptic potentiation / EPH-ephrin mediated repulsion of cells / positive regulation of cell adhesion / ephrin receptor signaling pathway / axonal growth cone / regulation of GTPase activity / protein tyrosine kinase binding / postsynaptic density membrane / integral component of postsynaptic membrane / dendritic shaft / negative regulation of cell migration / positive regulation of protein tyrosine kinase activity / filopodium / positive regulation of JUN kinase activity / ephrin receptor binding / Schaffer collateral - CA1 synapse / integral component of presynaptic membrane / adherens junction / neuromuscular junction / negative regulation of ERK1 and ERK2 cascade / axon guidance / receptor protein-tyrosine kinase / transmembrane receptor protein tyrosine kinase activity / cellular response to amyloid-beta / positive regulation of kinase activity / peptidyl-tyrosine phosphorylation / negative regulation of neuron projection development / amyloid-beta binding / kinase activity / transmembrane receptor protein tyrosine kinase signaling pathway / perikaryon / early endosome membrane / mitochondrial outer membrane / protein stabilization / dendritic spine / receptor complex / cell adhesion / positive regulation of cell migration / protein kinase activity / axon / neuron projection / protein autophosphorylation / glutamatergic synapse / dendrite / positive regulation of cell population proliferation / protein serine/threonine/tyrosine kinase activity / Golgi apparatus / cell surface / endoplasmic reticulum / integral component of plasma membrane / ATP binding / identical protein binding / plasma membrane / cytoplasm Similarity search - Function Ephrin type-A receptor 4, SAM domain / Ephrin type-A receptor 4, ligand binding domain / Ephrin receptor type-A /type-B / Ephrin receptor ligand binding domain / Ephrin receptor ligand binding domain / Eph receptor ligand-binding domain profile. / Receptor tyrosine kinase class V signature 2. / Ephrin type-A receptor 2 transmembrane domain / Ephrin receptor ligand binding domain / Receptor tyrosine kinase class V signature 1. ... Ephrin type-A receptor 4, SAM domain / Ephrin type-A receptor 4, ligand binding domain / Ephrin receptor type-A /type-B / Ephrin receptor ligand binding domain / Ephrin receptor ligand binding domain / Eph receptor ligand-binding domain profile. / Receptor tyrosine kinase class V signature 2. / Ephrin type-A receptor 2 transmembrane domain / Ephrin receptor ligand binding domain / Receptor tyrosine kinase class V signature 1. / Ephrin receptor, transmembrane domain / Tyrosine-protein kinase, receptor class V, conserved site / SAM domain (Sterile alpha motif) / Galactose-binding domain-like / SAM domain profile. / Sterile alpha motif. / Sterile alpha motif domain / Sterile alpha motif/pointed domain superfamily / Fibronectin type III domain / Fibronectin type 3 domain / Fibronectin type-III domain profile. / Fibronectin type III / Fibronectin type III superfamily / Galactose-binding-like domain superfamily / Tyrosine kinase, catalytic domain / Tyrosine-protein kinase, catalytic domain / Tyrosine protein kinases specific active-site signature. / Tyrosine-protein kinase, active site / Protein tyrosine and serine/threonine kinase / Serine-threonine/tyrosine-protein kinase, catalytic domain / Jelly Rolls / Serine/Threonine protein kinases, catalytic domain / Protein kinases ATP-binding region signature. / Protein kinase, ATP binding site / Immunoglobulin-like fold / Protein kinase domain profile. / Protein kinase domain / Protein kinase-like domain superfamily / Sandwich / Mainly Beta Similarity search - Domain/homologyBiological species Homo sapiens (human)Method X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution : 1.85 Å DetailsAuthors Bowden, T.A. / Aricescu, A.R. / Nettleship, J.E. / Siebold, C. / Rahman-Huq, N. / Owens, R.J. / Stuart, D.I. / Jones, E.Y. CitationJournal : Structure / Year : 2009Title : Structural Plasticity of Eph-Receptor A4 Facilitates Cross-Class Ephrin SignallingAuthors : Bowden, T.A. / Aricescu, A.R. / Nettleship, J.E. / Siebold, C. / Rahman-Huq, N. / Owens, R.J. / Stuart, D.I. / Jones, E.Y. History Deposition Jul 21, 2009 Deposition site : PDBE / Processing site : PDBERevision 1.0 Oct 27, 2009 Provider : repository / Type : Initial releaseRevision 1.1 Jul 13, 2011 Group : Advisory / Version format complianceRevision 1.2 Nov 23, 2011 Group : Database referencesRevision 1.3 Feb 28, 2018 Group : Source and taxonomy / Category : entity_src_genItem : _entity_src_gen.gene_src_common_name / _entity_src_gen.host_org_common_name ... _entity_src_gen.gene_src_common_name / _entity_src_gen.host_org_common_name / _entity_src_gen.pdbx_gene_src_scientific_name / _entity_src_gen.pdbx_host_org_cell_line / _entity_src_gen.pdbx_host_org_scientific_name / _entity_src_gen.pdbx_host_org_strain
Show all Show less Remark 700 SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED.