Entry | Database: PDB / ID: 2xvt |
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Title | Structure of the extracellular domain of human RAMP2 |
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Components | RECEPTOR ACTIVITY-MODIFYING PROTEIN 2 |
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Keywords | MEMBRANE PROTEIN / TRANSMEMBRANE / RECEPTOR TRANSPORT / PROTEIN-TRAFFICKING / GPCR / CRLR / CGRP / ADRENOMEDULIN |
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Function / homology | Function and homology information
basement membrane assembly / adrenomedullin binding / adrenomedullin receptor activity / adrenomedullin receptor complex / vascular associated smooth muscle cell development / adrenomedullin receptor signaling pathway / amylin receptor 2 signaling pathway / positive regulation of vasculogenesis / bicellular tight junction assembly / Calcitonin-like ligand receptors ...basement membrane assembly / adrenomedullin binding / adrenomedullin receptor activity / adrenomedullin receptor complex / vascular associated smooth muscle cell development / adrenomedullin receptor signaling pathway / amylin receptor 2 signaling pathway / positive regulation of vasculogenesis / bicellular tight junction assembly / Calcitonin-like ligand receptors / regulation of G protein-coupled receptor signaling pathway / negative regulation of vascular permeability / adherens junction assembly / sprouting angiogenesis / cellular response to vascular endothelial growth factor stimulus / negative regulation of endothelial cell apoptotic process / vasculogenesis / cellular response to hormone stimulus / coreceptor activity / clathrin-coated pit / protein localization to plasma membrane / intracellular protein transport / receptor internalization / regulation of blood pressure / adenylate cyclase-activating G protein-coupled receptor signaling pathway / positive regulation of angiogenesis / calcium ion transport / protein transport / heart development / High laminar flow shear stress activates signaling by PIEZO1 and PECAM1:CDH5:KDR in endothelial cells / angiogenesis / G alpha (s) signalling events / lysosome / receptor complex / G protein-coupled receptor signaling pathway / positive regulation of gene expression / cell surface / plasma membrane / cytoplasmSimilarity search - Function Receptor activity modifying family / Receptor activity modifying protein / RAMP domain superfamily / Receptor activity modifying family / DNA polymerase; domain 1 / Orthogonal Bundle / Mainly AlphaSimilarity search - Domain/homology |
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Biological species | HOMO SAPIENS (human) |
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Method | X-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 2.05 Å |
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Authors | Quigley, A. / Pike, A.C.W. / Burgess-Brown, N. / Krojer, T. / Shrestha, L. / Goubin, S. / Kim, J. / Das, S. / Muniz, J.R.C. / Canning, P. ...Quigley, A. / Pike, A.C.W. / Burgess-Brown, N. / Krojer, T. / Shrestha, L. / Goubin, S. / Kim, J. / Das, S. / Muniz, J.R.C. / Canning, P. / Chaikuad, A. / Vollmar, M. / von Delft, F. / Arrowsmith, C.H. / Weigelt, J. / Edwards, A.M. / Bountra, C. / Barr, A.J. / Carpenter, E.P. |
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Citation | Journal: To be Published Title: Structure of the Extracellular Domain of Human Ramp2 Authors: Quigley, A. / Pike, A.C.W. / Burgess-Brown, N. / Krojer, T. / Shrestha, L. / Goubin, S. / Kim, J. / Das, S. / Muniz, J.R.C. / Canning, P. / Chaikuad, A. / Vollmar, M. / von Delft, F. / ...Authors: Quigley, A. / Pike, A.C.W. / Burgess-Brown, N. / Krojer, T. / Shrestha, L. / Goubin, S. / Kim, J. / Das, S. / Muniz, J.R.C. / Canning, P. / Chaikuad, A. / Vollmar, M. / von Delft, F. / Arrowsmith, C.H. / Weigelt, J. / Edwards, A.M. / Bountra, C. / Barr, A.J. / Carpenter, E.P. |
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History | Deposition | Oct 31, 2010 | Deposition site: PDBE / Processing site: PDBE |
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Revision 1.0 | Dec 29, 2010 | Provider: repository / Type: Initial release |
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Revision 1.1 | Mar 6, 2013 | Group: Data collection |
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Revision 1.2 | Dec 10, 2014 | Group: Data collection / Version format compliance |
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Revision 1.3 | Jan 24, 2018 | Group: Database references / Category: citation_author / Item: _citation_author.name |
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Revision 1.4 | Nov 13, 2024 | Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other / Refinement description / Structure summary Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_entry_details / pdbx_modification_feature / pdbx_struct_conn_angle / struct_conn / struct_ncs_dom_lim / struct_site Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_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_asym_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_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_conn.ptnr2_label_seq_id / _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 / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id |
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