Entry Database : PDB / ID : 4xst Structure visualization Downloads & linksTitle Structure of the endoglycosidase-H treated L1-CR domains of the human insulin receptor in complex with residues 697-719 of the human insulin receptor (A-isoform) Components(Insulin receptor) x 2 Details Keywords Hormone/Hormone receptor / Insulin receptor / Insulin micro-receptor / Hormone-Hormone receptor complexFunction / homology Function and homology informationFunction Domain/homology Component
response to vanadate(3-) / Insulin receptor signalling cascade / Signaling by Insulin receptor / IRS activation / yolk / : / embryonic liver development / Insulin receptor recycling / 3-phosphoinositide-dependent protein kinase binding / Signal attenuation ... response to vanadate(3-) / Insulin receptor signalling cascade / Signaling by Insulin receptor / IRS activation / yolk / : / embryonic liver development / Insulin receptor recycling / 3-phosphoinositide-dependent protein kinase binding / Signal attenuation / positive regulation of glycoprotein biosynthetic process / PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling / response to resveratrol / lipoic acid binding / negative regulation of glycogen biosynthetic process / alternative mRNA splicing, via spliceosome / regulation of female gonad development / regulation of hydrogen peroxide metabolic process / positive regulation of meiotic cell cycle / cellular response to zinc ion starvation / positive regulation of developmental growth / insulin-like growth factor II binding / male sex determination / exocrine pancreas development / insulin receptor complex / insulin-like growth factor I binding / insulin receptor activity / response to vitamin D / negative regulation of transporter activity / positive regulation of kinase activity / positive regulation of protein-containing complex disassembly / response to manganese ion / cargo receptor activity / response to food / dendritic spine maintenance / insulin binding / PTB domain binding / regulation of gluconeogenesis / adrenal gland development / negative regulation of feeding behavior / neuronal cell body membrane / Signaling by Insulin receptor / response to testosterone / IRS activation / activation of protein kinase activity / protein tyrosine kinase activator activity / fat cell differentiation / amyloid-beta clearance / positive regulation of respiratory burst / response to starvation / positive regulation of receptor internalization / regulation of embryonic development / transport across blood-brain barrier / insulin receptor substrate binding / positive regulation of glycogen biosynthetic process / epidermis development / Signal attenuation / response to tumor necrosis factor / phosphatidylinositol 3-kinase binding / response to glucose / heart morphogenesis / peptidyl-tyrosine autophosphorylation / positive regulation of phosphorylation / response to glucocorticoid / dendrite membrane / cell surface receptor protein tyrosine kinase signaling pathway / Insulin receptor recycling / neuron projection maintenance / positive regulation of glycolytic process / activation of protein kinase B activity / positive regulation of mitotic nuclear division / Insulin receptor signalling cascade / response to nutrient levels / cerebellum development / : / receptor-mediated endocytosis / negative regulation of protein phosphorylation / response to hormone / liver development / learning / response to activity / molecular function activator activity / caveola / positive regulation of glucose import / liver regeneration / hippocampus development / animal organ morphogenesis / insulin-like growth factor receptor binding / positive regulation of MAP kinase activity / response to insulin / receptor internalization / receptor protein-tyrosine kinase / memory / cellular response to growth factor stimulus / peptidyl-tyrosine phosphorylation / cellular response to insulin stimulus / male gonad development / positive regulation of nitric oxide biosynthetic process / late endosome / insulin receptor signaling pathway Similarity search - Function 24 nucleotide stem-loop, u2 snrnp hairpin iv. U2 a'; Chain A / Receptor L-domain / Hormone Receptor, Insulin-like Growth Factor Receptor 1; Chain A domain 2 / Hormone Receptor, Insulin-like Growth Factor Receptor 1; Chain A, domain 2 / Insulin receptor, trans-membrane domain / Insulin receptor trans-membrane segment / Tyrosine-protein kinase, insulin-like receptor / Tyrosine-protein kinase, receptor class II, conserved site / Receptor tyrosine kinase class II signature. / Alpha-Beta Horseshoe ... 24 nucleotide stem-loop, u2 snrnp hairpin iv. U2 a'; Chain A / Receptor L-domain / Hormone Receptor, Insulin-like Growth Factor Receptor 1; Chain A domain 2 / Hormone Receptor, Insulin-like Growth Factor Receptor 1; Chain A, domain 2 / Insulin receptor, trans-membrane domain / Insulin receptor trans-membrane segment / Tyrosine-protein kinase, insulin-like receptor / Tyrosine-protein kinase, receptor class II, conserved site / Receptor tyrosine kinase class II signature. / Alpha-Beta Horseshoe / Receptor L-domain / Furin-like cysteine-rich domain / Receptor L-domain superfamily / Furin-like cysteine rich region / Receptor L domain / Furin-like repeat / Furin-like repeats / Growth factor receptor cysteine-rich domain superfamily / Fibronectin type III domain / Fibronectin type 3 domain / Fibronectin type-III domain profile. / Fibronectin type III / Fibronectin type III superfamily / Ribbon / Tyrosine-protein kinase, catalytic domain / Tyrosine 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 / Protein kinase, ATP binding site / Protein kinases ATP-binding region signature. / Immunoglobulin-like fold / Protein kinase domain profile. / Protein kinase domain / Protein kinase-like domain superfamily / Mainly Beta / Alpha Beta Similarity search - Domain/homologyBiological species Homo sapiens (human)Rattus norvegicus (Norway rat)Method X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution : 3 Å DetailsAuthors Menting, J.G. / Lawrence, C.F. / Kong, G.K.-W. / Lawrence, M.C. Funding support Australia, 2items Details Hide detailsOrganization Grant number Country National Health and Medical Research Council (NHMRC, Australia) APP1005896 Australia National Health and Medical Research Council (NHMRC, Australia) APP1058233 Australia
CitationJournal : Structure / Year : 2015Title : Structural Congruency of Ligand Binding to the Insulin and Insulin/Type 1 Insulin-like Growth Factor Hybrid Receptors.Authors : Menting, J.G. / Lawrence, C.F. / Kong, G.K. / Margetts, M.B. / Ward, C.W. / Lawrence, M.C. History Deposition Jan 22, 2015 Deposition site : RCSB / Processing site : RCSBRevision 1.0 Jun 10, 2015 Provider : repository / Type : Initial releaseRevision 1.1 Jul 22, 2015 Group : Database referencesRevision 1.2 Sep 13, 2017 Group : Author supporting evidence / Data collection ... Author supporting evidence / Data collection / Database references / Derived calculations / Source and taxonomy Category : citation / diffrn_source ... citation / diffrn_source / entity_src_gen / pdbx_audit_support / pdbx_entity_src_syn / pdbx_struct_assembly / pdbx_struct_assembly_gen / pdbx_struct_assembly_prop / pdbx_struct_oper_list Item : _citation.journal_id_CSD / _diffrn_source.pdbx_synchrotron_site ... _citation.journal_id_CSD / _diffrn_source.pdbx_synchrotron_site / _entity_src_gen.pdbx_alt_source_flag / _pdbx_audit_support.funding_organization / _pdbx_entity_src_syn.pdbx_alt_source_flag / _pdbx_struct_assembly.oligomeric_details / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_struct_assembly_prop.type / _pdbx_struct_assembly_prop.value / _pdbx_struct_oper_list.symmetry_operation Revision 1.3 Jan 8, 2020 Group : Author supporting evidence / Data collection / Category : chem_comp / pdbx_audit_supportItem : _chem_comp.type / _pdbx_audit_support.funding_organizationRevision 2.0 Jul 29, 2020 Group : Atomic model / Data collection ... Atomic model / Data collection / Derived calculations / Structure summary Category : atom_site / atom_site_anisotrop ... atom_site / atom_site_anisotrop / chem_comp / entity / pdbx_branch_scheme / pdbx_chem_comp_identifier / pdbx_entity_branch / pdbx_entity_branch_descriptor / pdbx_entity_branch_link / pdbx_entity_branch_list / pdbx_entity_nonpoly / pdbx_nonpoly_scheme / pdbx_struct_assembly_gen / struct_asym / struct_conn / struct_site / struct_site_gen Item : _atom_site.B_iso_or_equiv / _atom_site.Cartn_x ... _atom_site.B_iso_or_equiv / _atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _atom_site.auth_asym_id / _atom_site.auth_atom_id / _atom_site.auth_comp_id / _atom_site.auth_seq_id / _atom_site.label_asym_id / _atom_site.label_atom_id / _atom_site.label_comp_id / _atom_site.label_entity_id / _atom_site.type_symbol / _atom_site_anisotrop.U[1][1] / _atom_site_anisotrop.U[1][2] / _atom_site_anisotrop.U[1][3] / _atom_site_anisotrop.U[2][2] / _atom_site_anisotrop.U[2][3] / _atom_site_anisotrop.U[3][3] / _atom_site_anisotrop.pdbx_auth_asym_id / _atom_site_anisotrop.pdbx_auth_atom_id / _atom_site_anisotrop.pdbx_auth_comp_id / _atom_site_anisotrop.pdbx_auth_seq_id / _atom_site_anisotrop.pdbx_label_asym_id / _atom_site_anisotrop.pdbx_label_atom_id / _atom_site_anisotrop.pdbx_label_comp_id / _atom_site_anisotrop.type_symbol / _chem_comp.name / _chem_comp.type / _entity.formula_weight / _entity.pdbx_description / _entity.pdbx_number_of_molecules / _entity.src_method / _entity.type / _pdbx_struct_assembly_gen.asym_id_list / _struct_conn.pdbx_role / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id Description : Carbohydrate remediation / Provider : repository / Type : RemediationRevision 2.1 Sep 27, 2023 Group : Data collection / Database references ... Data collection / Database references / Derived calculations / Refinement description / Structure summary Category : chem_comp / chem_comp_atom ... chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_conn Item : _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI ... _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_conn.pdbx_leaving_atom_flag
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