Entry Database : PDB / ID : 3rg0 Structure visualization Downloads & linksTitle Structural and functional relationships between the lectin and arm domains of calreticulin ComponentsCalreticulin Details Keywords CHAPERONE / beta-sandwich / monoglucosylated proteins binding / carbohydrate binding / calcium binding / endoplasmic reticulumFunction / homology Function and homology informationFunction Domain/homology Component
Calnexin/calreticulin cycle / Scavenging by Class A Receptors / cytolytic granule / positive regulation of dendritic cell chemotaxis / cortical granule / negative regulation of trophoblast cell migration / negative regulation of retinoic acid receptor signaling pathway / cellular response to electrical stimulus / endoplasmic reticulum quality control compartment / regulation of meiotic nuclear division ... Calnexin/calreticulin cycle / Scavenging by Class A Receptors / cytolytic granule / positive regulation of dendritic cell chemotaxis / cortical granule / negative regulation of trophoblast cell migration / negative regulation of retinoic acid receptor signaling pathway / cellular response to electrical stimulus / endoplasmic reticulum quality control compartment / regulation of meiotic nuclear division / complement component C1q complex binding / response to glycoside / sarcoplasmic reticulum lumen / nuclear export signal receptor activity / negative regulation of intracellular steroid hormone receptor signaling pathway / hormone binding / cardiac muscle cell differentiation / molecular sequestering activity / Antigen Presentation: Folding, assembly and peptide loading of class I MHC / ER-Phagosome pathway / cortical actin cytoskeleton organization / nuclear androgen receptor binding / : / cellular response to lithium ion / response to testosterone / protein localization to nucleus / negative regulation of neuron differentiation / smooth endoplasmic reticulum / positive regulation of cell cycle / ERAD pathway / positive regulation of substrate adhesion-dependent cell spreading / positive regulation of phagocytosis / protein export from nucleus / phagocytic vesicle / positive regulation of endothelial cell migration / acrosomal vesicle / sarcoplasmic reticulum / peptide binding / peptide antigen assembly with MHC class I protein complex / MHC class I peptide loading complex / cellular response to virus / positive regulation of non-canonical NF-kappaB signal transduction / cellular senescence / unfolded protein binding / integrin binding / protein folding / response to estradiol / nuclear envelope / carbohydrate binding / spermatogenesis / collagen-containing extracellular matrix / protein stabilization / negative regulation of translation / ribosome / response to xenobiotic stimulus / iron ion binding / endoplasmic reticulum lumen / external side of plasma membrane / mRNA binding / ubiquitin protein ligase binding / calcium ion binding / positive regulation of cell population proliferation / positive regulation of gene expression / endoplasmic reticulum membrane / perinuclear region of cytoplasm / negative regulation of transcription by RNA polymerase II / cell surface / endoplasmic reticulum / protein-containing complex / extracellular space / extracellular region / membrane / cytosol Similarity search - Function Calreticulin / Calreticulin family repeated motif signature. / Calreticulin/calnexin / Calreticulin/calnexin, P domain superfamily / Calreticulin/calnexin, conserved site / Calreticulin family / Calreticulin family signature 1. / Calreticulin family signature 2. / Helix hairpin bin / Endoplasmic reticulum targeting sequence. ... Calreticulin / Calreticulin family repeated motif signature. / Calreticulin/calnexin / Calreticulin/calnexin, P domain superfamily / Calreticulin/calnexin, conserved site / Calreticulin family / Calreticulin family signature 1. / Calreticulin family signature 2. / Helix hairpin bin / Endoplasmic reticulum targeting sequence. / Jelly Rolls - #200 / Helix Hairpins / Concanavalin A-like lectin/glucanase domain superfamily / Jelly Rolls / Sandwich / Orthogonal Bundle / Mainly Beta / Mainly Alpha Similarity search - Domain/homologyBiological species Mus musculus (house mouse)Method X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution : 2.57 Å DetailsAuthors Kozlov, G. / Pocanschi, C.L. / Brockmeier, U. / Williams, D.B. / Gehring, K. CitationJournal : J.Biol.Chem. / Year : 2011Title : Structural and Functional Relationships between the Lectin and Arm Domains of Calreticulin.Authors : Pocanschi, C.L. / Kozlov, G. / Brockmeier, U. / Brockmeier, A. / Williams, D.B. / Gehring, K. History Deposition Apr 7, 2011 Deposition site : RCSB / Processing site : RCSBRevision 1.0 Jun 1, 2011 Provider : repository / Type : Initial releaseRevision 1.1 Jul 13, 2011 Group : Version format complianceRevision 1.2 Aug 31, 2011 Group : Database referencesRevision 1.3 Jul 26, 2017 Group : Refinement description / Source and taxonomy / Category : entity_src_gen / softwareRevision 1.4 Sep 13, 2023 Group : Data collection / Database references ... Data collection / Database references / Derived calculations / Refinement description Category : chem_comp_atom / chem_comp_bond ... chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / pdbx_struct_conn_angle / 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_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_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_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_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_conn.ptnr2_label_seq_id / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
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