Entry Database : PDB / ID : 3l2j Structure visualization Downloads & linksTitle Dimeric structure of the ligand-free extracellular domain of the human parathyroid hormone receptor (PTH1R) ComponentsFusion protein of Maltose-binding periplasmic protein and Parathyroid hormone/parathyroid hormone-related peptide receptor Details Keywords MEMBRANE PROTEIN / dimer / extracellular domain / MBP fusion protein / Periplasm / Sugar transport / Transport / Cell membrane / Disease mutation / Disulfide bond / Dwarfism / G-protein coupled receptor / Glycoprotein / Membrane / Receptor / Transducer / TransmembraneFunction / homology Function and homology informationFunction Domain/homology Component
parathyroid hormone receptor activity / G protein-coupled peptide receptor activity / Class B/2 (Secretin family receptors) / osteoblast development / positive regulation of inositol phosphate biosynthetic process / detection of maltose stimulus / maltose binding / maltose transport complex / maltose transport / maltodextrin transmembrane transport ... parathyroid hormone receptor activity / G protein-coupled peptide receptor activity / Class B/2 (Secretin family receptors) / osteoblast development / positive regulation of inositol phosphate biosynthetic process / detection of maltose stimulus / maltose binding / maltose transport complex / maltose transport / maltodextrin transmembrane transport / bone mineralization / G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger / peptide hormone binding / carbohydrate transmembrane transporter activity / ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing / carbohydrate transport / chondrocyte differentiation / cell maturation / bone resorption / ATP-binding cassette (ABC) transporter complex / cell chemotaxis / skeletal system development / adenylate cyclase-modulating G protein-coupled receptor signaling pathway / adenylate cyclase-activating G protein-coupled receptor signaling pathway / intracellular calcium ion homeostasis / : / phospholipase C-activating G protein-coupled receptor signaling pathway / outer membrane-bounded periplasmic space / G alpha (s) signalling events / basolateral plasma membrane / cell population proliferation / in utero embryonic development / periplasmic space / cell surface receptor signaling pathway / receptor complex / apical plasma membrane / G protein-coupled receptor signaling pathway / negative regulation of cell population proliferation / DNA damage response / positive regulation of cell population proliferation / protein homodimerization activity / membrane / nucleus / plasma membrane / cytoplasm Similarity search - Function GPCR, family 2, extracellular hormone receptor domain / Hormone receptor fold / GPCR, family 2, parathyroid hormone receptor / G-protein coupled receptors family 2 signature 1. / Hormone receptor domain / GPCR, family 2, extracellular hormone receptor domain / G-protein coupled receptors family 2 profile 1. / Domain present in hormone receptors / GPCR family 2, extracellular hormone receptor domain superfamily / G-protein coupled receptors family 2 signature 2. ... GPCR, family 2, extracellular hormone receptor domain / Hormone receptor fold / GPCR, family 2, parathyroid hormone receptor / G-protein coupled receptors family 2 signature 1. / Hormone receptor domain / GPCR, family 2, extracellular hormone receptor domain / G-protein coupled receptors family 2 profile 1. / Domain present in hormone receptors / GPCR family 2, extracellular hormone receptor domain superfamily / G-protein coupled receptors family 2 signature 2. / GPCR, family 2, secretin-like, conserved site / GPCR, family 2, secretin-like / 7 transmembrane receptor (Secretin family) / GPCR, family 2-like / G-protein coupled receptors family 2 profile 2. / Maltose/Cyclodextrin ABC transporter, substrate-binding protein / Solute-binding family 1, conserved site / Bacterial extracellular solute-binding proteins, family 1 signature. / Bacterial extracellular solute-binding protein / Bacterial extracellular solute-binding protein / Few Secondary Structures / Irregular Similarity search - Domain/homology alpha-maltose / Maltose/maltodextrin-binding periplasmic protein / Parathyroid hormone/parathyroid hormone-related peptide receptor Similarity search - ComponentBiological species Escherichia coli (E. coli)Homo sapiens (human)Method X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution : 3.24 Å DetailsAuthors Pioszak, A.A. / Xu, H.E. CitationJournal : J.Biol.Chem. / Year : 2010Title : Dimeric arrangement of the parathyroid hormone receptor and a structural mechanism for ligand-induced dissociation.Authors : Pioszak, A.A. / Harikumar, K.G. / Parker, N.R. / Miller, L.J. / Xu, H.E. History Deposition Dec 15, 2009 Deposition site : RCSB / Processing site : RCSBRevision 1.0 Feb 2, 2010 Provider : repository / Type : Initial releaseRevision 1.1 Jul 13, 2011 Group : Version format complianceRevision 1.2 Aug 2, 2017 Group : Refinement description / Source and taxonomy / Category : entity_src_gen / softwareRevision 2.0 Jul 29, 2020 Group : Atomic model / Data collection ... Atomic model / Data collection / Database references / Derived calculations / Non-polymer description / Structure summary Category : atom_site / atom_site_anisotrop ... atom_site / atom_site_anisotrop / chem_comp / entity / entity_name_com / 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_molecule_features / pdbx_nonpoly_scheme / struct_conn / struct_conn_type / struct_ref_seq_dif / 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_atom_id / _atom_site.label_comp_id / _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_atom_id / _atom_site_anisotrop.pdbx_label_comp_id / _chem_comp.formula / _chem_comp.formula_weight / _chem_comp.id / _chem_comp.mon_nstd_flag / _chem_comp.name / _chem_comp.type / _entity.formula_weight / _entity.pdbx_description / _entity.type / _struct_ref_seq_dif.details Description : Carbohydrate remediation / Provider : repository / Type : RemediationRevision 2.1 Sep 6, 2023 Group : Data collection / Database references ... Data collection / Database references / 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_ncs_dom_lim Item : _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI ... _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id
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