Entry | Database: PDB / ID: 3rjr |
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Title | Crystal Structure of pro-TGF beta 1 |
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Components | Transforming growth factor beta-1 |
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Keywords | CYTOKINE / TGF beta / activation / integrin |
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Function / homology | Function and homology information
Platelet degranulation / Cell surface interactions at the vascular wall / Molecules associated with elastic fibres / TGF-beta receptor signaling activates SMADs / Syndecan interactions / RUNX3 regulates CDKN1A transcription / RUNX3 regulates p14-ARF / Downregulation of TGF-beta receptor signaling / TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition) / Regulation of RUNX3 expression and activity ...Platelet degranulation / Cell surface interactions at the vascular wall / Molecules associated with elastic fibres / TGF-beta receptor signaling activates SMADs / Syndecan interactions / RUNX3 regulates CDKN1A transcription / RUNX3 regulates p14-ARF / Downregulation of TGF-beta receptor signaling / TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition) / Regulation of RUNX3 expression and activity / regulation of binding / regulation of DNA binding / positive regulation of microglia differentiation / negative regulation of skeletal muscle tissue development / regulation of striated muscle tissue development / regulation of protein import into nucleus / type III transforming growth factor beta receptor binding / negative regulation of hyaluronan biosynthetic process / extracellular matrix assembly / negative regulation of macrophage cytokine production / odontoblast differentiation / positive regulation of isotype switching to IgA isotypes / membrane protein intracellular domain proteolysis / hyaluronan catabolic process / regulation of transforming growth factor beta receptor signaling pathway / ATP biosynthetic process / receptor catabolic process / type II transforming growth factor beta receptor binding / type I transforming growth factor beta receptor binding / positive regulation of chemotaxis / negative regulation of myoblast differentiation / cell-cell junction organization / response to cholesterol / positive regulation of fibroblast migration / phosphate-containing compound metabolic process / positive regulation of epidermal growth factor receptor signaling pathway / negative regulation of cell-cell adhesion / negative regulation of fat cell differentiation / positive regulation of interleukin-17 production / positive regulation of SMAD protein signal transduction / negative regulation of blood vessel endothelial cell migration / positive regulation of cell division / negative regulation of cell cycle / positive regulation of collagen biosynthetic process / positive regulation of blood vessel endothelial cell migration / epithelial to mesenchymal transition / lymph node development / chondrocyte differentiation / hematopoietic progenitor cell differentiation / positive regulation of epithelial to mesenchymal transition / salivary gland morphogenesis / extrinsic apoptotic signaling pathway / positive regulation of protein dephosphorylation / cellular response to transforming growth factor beta stimulus / positive regulation of protein metabolic process / transforming growth factor beta receptor signaling pathway / extracellular matrix / positive regulation of superoxide anion generation / negative regulation of protein phosphorylation / cytokine activity / response to progesterone / positive regulation of protein secretion / antigen binding / growth factor activity / positive regulation of protein-containing complex assembly / negative regulation of cell growth / response to wounding / positive regulation of protein import into nucleus / negative regulation of epithelial cell proliferation / response to estradiol / regulation of cell population proliferation / positive regulation of ERK1 and ERK2 cascade / blood microparticle / positive regulation of cell migration / inflammatory response / negative regulation of cell population proliferation / protein phosphorylation / negative regulation of gene expression / negative regulation of DNA-templated transcription / positive regulation of cell population proliferation / positive regulation of gene expression / positive regulation of DNA-templated transcription / cell surface / positive regulation of transcription by RNA polymerase II / extracellular space / identical protein binding / nucleus / cytoplasmSimilarity search - Function Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #2330 / Jelly Rolls - #970 / Transforming growth factor beta-1 proprotein / Transforming growth factor-beta / TGF-beta, propeptide / TGF-beta propeptide / Transforming growth factor beta, conserved site / TGF-beta family signature. / Transforming growth factor-beta-related / Transforming growth factor-beta (TGF-beta) family ...Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #2330 / Jelly Rolls - #970 / Transforming growth factor beta-1 proprotein / Transforming growth factor-beta / TGF-beta, propeptide / TGF-beta propeptide / Transforming growth factor beta, conserved site / TGF-beta family signature. / Transforming growth factor-beta-related / Transforming growth factor-beta (TGF-beta) family / Transforming growth factor-beta, C-terminal / Transforming growth factor beta like domain / TGF-beta family profile. / Cystine Knot Cytokines, subunit B / Cystine-knot cytokines / Cystine-knot cytokine / Single alpha-helices involved in coiled-coils or other helix-helix interfaces / Helix non-globular / Special / Ribbon / Jelly Rolls / Sandwich / Mainly BetaSimilarity search - Domain/homology |
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Biological species | ![](img/tx_mammal.gif) Sus scrofa (pig) |
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Method | X-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 3.05 Å |
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Authors | Zhu, J.H. / Shi, M.L. / Springer, T.A. |
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Citation | Journal: Nature / Year: 2011 Title: Latent TGF-Beta structure and activation Authors: Shi, M. / Zhu, J. / Wang, R. / Chen, X. / Mi, L. / Walz, T. / Springer, T.A. |
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History | Deposition | Apr 15, 2011 | Deposition site: RCSB / Processing site: RCSB |
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Revision 1.0 | Jun 15, 2011 | Provider: repository / Type: Initial release |
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Revision 1.1 | Jul 13, 2011 | Group: Version format compliance |
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Revision 1.2 | Feb 13, 2013 | Group: Database references |
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Revision 1.3 | Nov 8, 2017 | Group: Refinement description / Category: software |
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Revision 2.0 | Jul 29, 2020 | Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Database references / Derived calculations / Structure summary Category: atom_site / chem_comp ...atom_site / chem_comp / entity / 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_nonpoly_scheme / pdbx_struct_assembly_gen / pdbx_validate_close_contact / struct_asym / struct_conn / 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_seq_id / _atom_site.label_asym_id / _atom_site.label_entity_id / _chem_comp.name / _chem_comp.type / _pdbx_entity_nonpoly.entity_id / _pdbx_entity_nonpoly.name / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_validate_close_contact.auth_asym_id_2 / _pdbx_validate_close_contact.auth_seq_id_2 / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.pdbx_role / _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_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_ref_seq_dif.details Description: Carbohydrate remediation / Provider: repository / Type: Remediation |
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