登録情報 データベース : PDB / ID : 2wo1 構造の表示 ダウンロードとリンクタイトル Crystal Structure of the EphA4 Ligand Binding Domain 要素EPHRIN TYPE-A RECEPTOR 詳細 キーワード TRANSFERASE / GLYCOPROTEIN / AXON GUIDANCE / VASCULAR DEVELOPMENT / CELL SURFACE RECEPTOR / CELL SIGNALING機能・相同性 機能・相同性情報分子機能 ドメイン・相同性 構成要素
DH domain binding / neuron projection fasciculation / positive regulation of Rho guanyl-nucleotide exchange factor activity / corticospinal tract morphogenesis / regulation of astrocyte differentiation / negative regulation of proteolysis involved in protein catabolic process / neuron projection guidance / nephric duct morphogenesis / fasciculation of sensory neuron axon / fasciculation of motor neuron axon ... DH domain binding / neuron projection fasciculation / positive regulation of Rho guanyl-nucleotide exchange factor activity / corticospinal tract morphogenesis / regulation of astrocyte differentiation / negative regulation of proteolysis involved in protein catabolic process / neuron projection guidance / nephric duct morphogenesis / fasciculation of sensory neuron axon / fasciculation of motor neuron axon / regulation of synapse pruning / synapse pruning / positive regulation of aspartic-type endopeptidase activity involved in amyloid precursor protein catabolic process / negative regulation of cellular response to hypoxia / negative regulation of axon regeneration / glial cell migration / transmembrane-ephrin receptor activity / PH domain binding / GPI-linked ephrin receptor activity / regulation of modification of synaptic structure / regulation of dendritic spine morphogenesis / negative regulation of cell adhesion / negative regulation of epithelial to mesenchymal transition / motor neuron axon guidance / adult walking behavior / adherens junction organization / positive regulation of dendrite morphogenesis / EPH-Ephrin signaling / Somitogenesis / positive regulation of amyloid-beta formation / regulation of axonogenesis / cochlea development / regulation of GTPase activity / EPHA-mediated growth cone collapse / positive regulation of protein tyrosine kinase activity / positive regulation of cell adhesion / negative regulation of long-term synaptic potentiation / EPH-ephrin mediated repulsion of cells / ephrin receptor signaling pathway / axonal growth cone / axon terminus / ephrin receptor binding / protein tyrosine kinase binding / negative regulation of cell migration / filopodium / dendritic shaft / axon guidance / receptor protein-tyrosine kinase / adherens junction / postsynaptic density membrane / neuromuscular junction / peptidyl-tyrosine phosphorylation / Schaffer collateral - CA1 synapse / negative regulation of ERK1 and ERK2 cascade / cellular response to amyloid-beta / negative regulation of neuron projection development / early endosome membrane / kinase activity / presynaptic membrane / amyloid-beta binding / protein tyrosine kinase activity / perikaryon / protein autophosphorylation / mitochondrial outer membrane / dendritic spine / protein stabilization / negative regulation of translation / cell adhesion / positive regulation of cell migration / protein kinase activity / axon / positive regulation of cell population proliferation / glutamatergic synapse / dendrite / cell surface / ATP binding / identical protein binding / plasma membrane / cytoplasm 類似検索 - 分子機能 Ephrin type-A receptor 4, SAM domain / Ephrin type-A receptor 4, ligand binding domain / Tyrosine-protein kinase ephrin type A/B receptor-like / Tyrosine-protein kinase ephrin type A/B receptor-like / : / Ephrin receptor type-A /type-B / Ephrin receptor ligand binding domain / Tyrosine-protein kinase, receptor class V, conserved site / Ephrin receptor, transmembrane domain / Ephrin receptor ligand binding domain ... Ephrin type-A receptor 4, SAM domain / Ephrin type-A receptor 4, ligand binding domain / Tyrosine-protein kinase ephrin type A/B receptor-like / Tyrosine-protein kinase ephrin type A/B receptor-like / : / Ephrin receptor type-A /type-B / Ephrin receptor ligand binding domain / Tyrosine-protein kinase, receptor class V, conserved site / Ephrin receptor, transmembrane domain / Ephrin receptor ligand binding domain / Ephrin type-A receptor 2 transmembrane domain / Receptor tyrosine kinase class V signature 1. / Receptor tyrosine kinase class V signature 2. / Eph receptor ligand-binding domain profile. / Ephrin receptor ligand binding domain / Putative ephrin-receptor like / 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. / Galactose-binding-like domain superfamily / Fibronectin type III / Fibronectin type III superfamily / Tyrosine-protein kinase, catalytic domain / Tyrosine kinase, catalytic domain / Tyrosine protein kinases specific active-site signature. / Tyrosine-protein kinase, active site / Serine-threonine/tyrosine-protein kinase, catalytic domain / Protein tyrosine and serine/threonine kinase / Jelly Rolls / Serine/Threonine protein kinases, catalytic domain / Protein kinase, ATP binding site / Protein kinases ATP-binding region signature. / Protein kinase domain profile. / Protein kinase domain / Immunoglobulin-like fold / Protein kinase-like domain superfamily / Sandwich / Mainly Beta 類似検索 - ドメイン・相同性生物種 Homo sapiens (ヒト)手法 X線回折 / シンクロトロン / 分子置換 / 解像度 : 1.85 Å 詳細データ登録者 Bowden, T.A. / Aricescu, A.R. / Nettleship, J.E. / Siebold, C. / Rahman-Huq, N. / Owens, R.J. / Stuart, D.I. / Jones, E.Y. 引用ジャーナル : Structure / 年 : 2009タイトル : Structural Plasticity of Eph-Receptor A4 Facilitates Cross-Class Ephrin Signalling著者 : Bowden, T.A. / Aricescu, A.R. / Nettleship, J.E. / Siebold, C. / Rahman-Huq, N. / Owens, R.J. / Stuart, D.I. / Jones, E.Y. 履歴 登録 2009年7月21日 登録サイト : PDBE / 処理サイト : PDBE改定 1.0 2009年10月27日 Provider : repository / タイプ : Initial release改定 1.1 2011年7月13日 Group : Advisory / Version format compliance改定 1.2 2011年11月23日 Group : Database references改定 1.3 2018年2月28日 Group : Source and taxonomy / カテゴリ : 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 改定 1.4 2023年12月20日 Group : Data collection / Database references ... Data collection / Database references / Derived calculations / Other / Refinement description カテゴリ : chem_comp_atom / chem_comp_bond ... chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_initial_refinement_model / struct_site Item : _database_2.pdbx_DOI / _database_2.pdbx_database_accession ... _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
すべて表示 表示を減らす 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.