Entry Database : PDB / ID : 3ff8 Structure visualization Downloads & linksTitle Structure of NK cell receptor KLRG1 bound to E-cadherin ComponentsEpithelial cadherin Killer cell lectin-like receptor subfamily G member 1 DetailsKeywords Cell Adhesion/Immune System / KLRG1-cadherin complex / Calcium / Cell adhesion / Cell junction / Cell membrane / Cleavage on pair of basic residues / Disease mutation / Glycoprotein / Membrane / Phosphoprotein / Polymorphism / Transmembrane / Lectin / Receptor / Signal-anchor / Cell Adhesion-Immune System COMPLEXFunction / homology Function and homology informationFunction Domain/homology Component
response to Gram-positive bacterium / regulation of protein catabolic process at postsynapse, modulating synaptic transmission / pituitary gland development / gamma-catenin binding / negative regulation of axon extension / cell-cell adhesion mediated by cadherin / cellular response to indole-3-methanol / flotillin complex / calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules / Formation of definitive endoderm ... response to Gram-positive bacterium / regulation of protein catabolic process at postsynapse, modulating synaptic transmission / pituitary gland development / gamma-catenin binding / negative regulation of axon extension / cell-cell adhesion mediated by cadherin / cellular response to indole-3-methanol / flotillin complex / calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules / Formation of definitive endoderm / Adherens junctions interactions / catenin complex / Apoptotic cleavage of cell adhesion proteins / GTPase activating protein binding / cell-cell junction assembly / adherens junction organization / apical junction complex / ankyrin binding / negative regulation of cell-cell adhesion / cellular response to lithium ion / homophilic cell adhesion via plasma membrane adhesion molecules / lateral plasma membrane / RHO GTPases activate IQGAPs / Integrin cell surface interactions / cell adhesion molecule binding / synapse assembly / InlA-mediated entry of Listeria monocytogenes into host cells / Degradation of the extracellular matrix / negative regulation of cell migration / protein tyrosine kinase binding / protein localization to plasma membrane / adherens junction / cell morphogenesis / trans-Golgi network / cytoplasmic side of plasma membrane / response to toxic substance / beta-catenin binding / cell-cell adhesion / positive regulation of protein import into nucleus / neuron projection development / Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell / actin cytoskeleton / lamellipodium / cell junction / carbohydrate binding / postsynapse / regulation of gene expression / cell surface receptor signaling pathway / endosome / response to xenobiotic stimulus / cadherin binding / intracellular membrane-bounded organelle / innate immune response / glutamatergic synapse / calcium ion binding / positive regulation of DNA-templated transcription / perinuclear region of cytoplasm / extracellular exosome / extracellular region / identical protein binding / membrane / plasma membrane Similarity search - Function Killer cell lectin-like receptor subfamily G member 1 / Cadherin prodomain like / Cadherin prodomain / Cadherin prodomain like / Natural killer cell receptor-like, C-type lectin-like domain / Cadherin, Y-type LIR-motif / Cadherin, Y-type LIR-motif / Catenin binding domain superfamily / Cadherins / Cadherin ... Killer cell lectin-like receptor subfamily G member 1 / Cadherin prodomain like / Cadherin prodomain / Cadherin prodomain like / Natural killer cell receptor-like, C-type lectin-like domain / Cadherin, Y-type LIR-motif / Cadherin, Y-type LIR-motif / Catenin binding domain superfamily / Cadherins / Cadherin / Cadherin conserved site / Cadherin domain signature. / Cadherin repeats. / Cadherin domain / Cadherins domain profile. / Cadherin-like / Cadherin-like superfamily / Mannose-Binding Protein A; Chain A / Mannose-Binding Protein A, subunit A / Lectin C-type domain / C-type lectin domain profile. / C-type lectin-like / C-type lectin (CTL) or carbohydrate-recognition domain (CRD) / C-type lectin-like/link domain superfamily / C-type lectin fold / Roll / Immunoglobulin-like / Sandwich / Mainly Beta / Alpha Beta Similarity search - Domain/homologyBiological species Homo sapiens (human)Mus musculus (house mouse)Method X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution : 2 Å DetailsAuthors Li, Y. / Mariuzza, R.A. CitationJournal : Immunity / Year : 2009Title : Structure of natural killer cell receptor KLRG1 bound to E-cadherin reveals basis for MHC-independent missing self recognition.Authors : Li, Y. / Hofmann, M. / Wang, Q. / Teng, L. / Chlewicki, L.K. / Pircher, H. / Mariuzza, R.A. History Deposition Dec 2, 2008 Deposition site : RCSB / Processing site : RCSBRevision 1.0 Jul 28, 2009 Provider : repository / Type : Initial releaseRevision 1.1 Jul 13, 2011 Group : Version format complianceRevision 1.2 Nov 1, 2017 Group : Advisory / Refinement description / Category : pdbx_unobs_or_zero_occ_atoms / softwareItem : _software.classification / _software.contact_author ... _software.classification / _software.contact_author / _software.contact_author_email / _software.date / _software.language / _software.location / _software.name / _software.type / _software.version Revision 1.3 Oct 20, 2021 Group : Advisory / Database references / Derived calculationsCategory : database_2 / pdbx_struct_conn_angle ... database_2 / pdbx_struct_conn_angle / pdbx_unobs_or_zero_occ_atoms / struct_conn / struct_ref_seq_dif / struct_site Item : _database_2.pdbx_DOI / _database_2.pdbx_database_accession ... _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id Revision 1.4 Sep 6, 2023 Group : Data collection / Refinement descriptionCategory : chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model
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