Entry Database : PDB / ID : 2fyl Structure visualization Downloads & linksTitle Haddock model of the complex between double module of LRP, CR56, and first domain of receptor associated protein, RAP-d1. ComponentsAlpha-2-macroglobulin receptor-associated protein Low-density lipoprotein receptor-related protein 1 DetailsKeywords SURFACE ACTIVE PROTEIN / Complex / shift-mapping / haddock / interfaceFunction / homology Function and homology informationFunction Domain/homology Component
alpha-2 macroglobulin receptor activity / apolipoprotein receptor activity / positive regulation of lipid transport / regulation of phospholipase A2 activity / extracellular negative regulation of signal transduction / positive regulation of transcytosis / lipoprotein particle receptor binding / negative regulation of platelet-derived growth factor receptor-beta signaling pathway / negative regulation of metallopeptidase activity / lipase binding ... alpha-2 macroglobulin receptor activity / apolipoprotein receptor activity / positive regulation of lipid transport / regulation of phospholipase A2 activity / extracellular negative regulation of signal transduction / positive regulation of transcytosis / lipoprotein particle receptor binding / negative regulation of platelet-derived growth factor receptor-beta signaling pathway / negative regulation of metallopeptidase activity / lipase binding / negative regulation of very-low-density lipoprotein particle clearance / regulation of receptor-mediated endocytosis / positive regulation of lysosomal protein catabolic process / rough endoplasmic reticulum lumen / aorta morphogenesis / negative regulation of smooth muscle cell migration / regulation of cholesterol transport / receptor antagonist activity / clathrin heavy chain binding / amyloid-beta clearance by transcytosis / low-density lipoprotein particle receptor activity / regulation of extracellular matrix disassembly / negative regulation of amyloid-beta clearance / amyloid-beta clearance by cellular catabolic process / scavenger receptor activity / very-low-density lipoprotein particle receptor binding / plasma membrane protein complex / positive regulation of amyloid-beta clearance / transcytosis / cis-Golgi network / negative regulation of receptor internalization / heparan sulfate proteoglycan binding / astrocyte activation involved in immune response / apoptotic cell clearance / cargo receptor activity / retinoid metabolic process / lysosomal transport / microtubule organizing center / lipoprotein transport / low-density lipoprotein particle receptor binding / enzyme-linked receptor protein signaling pathway / negative regulation of SMAD protein signal transduction / negative regulation of Wnt signaling pathway / amyloid-beta clearance / positive regulation of endocytosis / apolipoprotein binding / transport across blood-brain barrier / endoplasmic reticulum-Golgi intermediate compartment / positive regulation of cholesterol efflux / endomembrane system / Scavenging of heme from plasma / phagocytosis / Retinoid metabolism and transport / clathrin-coated pit / receptor-mediated endocytosis / negative regulation of protein binding / endosome lumen / regulation of actin cytoskeleton organization / positive regulation of protein localization to plasma membrane / lipid metabolic process / receptor internalization / Golgi lumen / cellular response to amyloid-beta / endocytic vesicle membrane / positive regulation of protein binding / signaling receptor activity / heparin binding / amyloid-beta binding / basolateral plasma membrane / receptor ligand activity / early endosome / receptor complex / endosome / lysosomal membrane / negative regulation of gene expression / focal adhesion / signaling receptor binding / calcium ion binding / protein-containing complex binding / Golgi apparatus / cell surface / endoplasmic reticulum / signal transduction / RNA binding / extracellular region / membrane / nucleus / plasma membrane Similarity search - Function Domain of unknown function DUF5050 / Domain of unknown function (DUF5050) / RAP domain / Receptor-associated Protein / Alpha-2-macroglobulin receptor-associated protein, domain 1 / Alpha-2-macroglobulin RAP, C-terminal / RAP domain superfamily / Alpha-2-macroglobulin RAP, domain 3 / Alpha-2-macroglobulin RAP, domain 2 / Alpha-2-macroglobulin receptor-associated protein ... Domain of unknown function DUF5050 / Domain of unknown function (DUF5050) / RAP domain / Receptor-associated Protein / Alpha-2-macroglobulin receptor-associated protein, domain 1 / Alpha-2-macroglobulin RAP, C-terminal / RAP domain superfamily / Alpha-2-macroglobulin RAP, domain 3 / Alpha-2-macroglobulin RAP, domain 2 / Alpha-2-macroglobulin receptor-associated protein / Alpha-2-macroglobulin RAP, N-terminal domain / Alpha-2-macroglobulin RAP, C-terminal domain / Complement Clr-like EGF domain / Complement Clr-like EGF-like / Low-density lipoprotein receptor repeat class B / LDL-receptor class B (LDLRB) repeat profile. / LDLR class B repeat / Low-density lipoprotein-receptor YWTD domain / Low-density lipoprotein receptor domain class A / Endoplasmic reticulum targeting sequence. / : / Low-density lipoprotein (LDL) receptor class A, conserved site / LDL-receptor class A (LDLRA) domain signature. / LDL-receptor class A (LDLRA) domain profile. / Calcium-binding EGF domain / Low-density lipoprotein receptor domain class A / Low-density lipoprotein (LDL) receptor class A repeat / LDL receptor-like superfamily / Six-bladed beta-propeller, TolB-like / Coagulation Factor Xa inhibitory site / EGF-type aspartate/asparagine hydroxylation site / EGF-like calcium-binding, conserved site / Calcium-binding EGF-like domain signature. / Aspartic acid and asparagine hydroxylation site. / EGF-like calcium-binding domain / Calcium-binding EGF-like domain / Epidermal growth factor-like domain. / EGF-like domain profile. / Growth factor receptor cysteine-rich domain superfamily / EGF-like domain signature 2. / EGF-like domain signature 1. / EGF-like domain / Up-down Bundle / Mainly Alpha Similarity search - Domain/homologyBiological species Homo sapiens (human)Method SOLUTION NMR / HADDOCK modelling from chemical shift perturbation data on both complex partners DetailsAuthors Jensen, G.A. / Andersen, O.M. / Bonvin, A.M. / Bjerrum-Bohr, I. / Etzerodt, M. / O'shea, C. / Poulsen, F.M. / Kragelund, B.B. CitationJournal : J.Mol.Biol. / Year : 2006Title : Binding Site Structure of One LRP-RAP Complex:Implications for a Common Ligand-Receptor Binding Motif.Authors : Jensen, G.A. / Andersen, O.M. / Bonvin, A.M. / Bjerrum-Bohr, I. / Etzerodt, M. / O'shea, C. / Poulsen, F.M. / Kragelund, B.B. History Deposition Feb 8, 2006 Deposition site : RCSB / Processing site : RCSBRevision 1.0 Oct 10, 2006 Provider : repository / Type : Initial releaseRevision 1.1 May 1, 2008 Group : Version format complianceRevision 1.2 Jul 13, 2011 Group : Version format complianceRevision 1.3 Mar 9, 2022 Group : Database references / Derived calculationsCategory : database_2 / pdbx_struct_assembly ... database_2 / pdbx_struct_assembly / pdbx_struct_conn_angle / pdbx_struct_oper_list / struct_conn / 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.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_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_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_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
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