Entry | Database: PDB / ID: 4mrc |
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Title | Human Transthyretin Ser52Pro Mutant |
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Components | Transthyretin |
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Keywords | TRANSPORT PROTEIN / Hormone Transporter / Thyroxine T4 |
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Function / homology | Function and homology information
Retinoid cycle disease events / The canonical retinoid cycle in rods (twilight vision) / thyroid hormone binding / purine nucleobase metabolic process / Non-integrin membrane-ECM interactions / Retinoid metabolism and transport / hormone activity / azurophil granule lumen / Amyloid fiber formation / Neutrophil degranulation ...Retinoid cycle disease events / The canonical retinoid cycle in rods (twilight vision) / thyroid hormone binding / purine nucleobase metabolic process / Non-integrin membrane-ECM interactions / Retinoid metabolism and transport / hormone activity / azurophil granule lumen / Amyloid fiber formation / Neutrophil degranulation / extracellular space / extracellular exosome / extracellular region / identical protein bindingSimilarity search - Function Transthyretin/hydroxyisourate hydrolase domain / Transthyretin, conserved site / Transthyretin signature 2. / Transthyretin, thyroxine binding site / Transthyretin signature 1. / Transthyretin / Transthyretin/hydroxyisourate hydrolase / Transthyretin/hydroxyisourate hydrolase domain / Transthyretin/hydroxyisourate hydrolase domain superfamily / HIUase/Transthyretin family ...Transthyretin/hydroxyisourate hydrolase domain / Transthyretin, conserved site / Transthyretin signature 2. / Transthyretin, thyroxine binding site / Transthyretin signature 1. / Transthyretin / Transthyretin/hydroxyisourate hydrolase / Transthyretin/hydroxyisourate hydrolase domain / Transthyretin/hydroxyisourate hydrolase domain superfamily / HIUase/Transthyretin family / Immunoglobulin-like / Sandwich / Mainly BetaSimilarity search - Domain/homology |
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Biological species | Homo sapiens (human) |
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Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.54 Å |
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Authors | Chen, W.J. / Wood, S.P. |
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Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 2014 Title: Proteolytic cleavage of Ser52Pro variant transthyretin triggers its amyloid fibrillogenesis. Authors: Mangione, P.P. / Porcari, R. / Gillmore, J.D. / Pucci, P. / Monti, M. / Porcari, M. / Giorgetti, S. / Marchese, L. / Raimondi, S. / Serpell, L.C. / Chen, W. / Relini, A. / Marcoux, J. / ...Authors: Mangione, P.P. / Porcari, R. / Gillmore, J.D. / Pucci, P. / Monti, M. / Porcari, M. / Giorgetti, S. / Marchese, L. / Raimondi, S. / Serpell, L.C. / Chen, W. / Relini, A. / Marcoux, J. / Clatworthy, I.R. / Taylor, G.W. / Tennent, G.A. / Robinson, C.V. / Hawkins, P.N. / Stoppini, M. / Wood, S.P. / Pepys, M.B. / Bellotti, V. |
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History | Deposition | Sep 17, 2013 | Deposition site: RCSB / Processing site: RCSB |
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Revision 1.0 | Jan 8, 2014 | Provider: repository / Type: Initial release |
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Revision 1.1 | Jan 15, 2014 | Group: Database references |
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Revision 1.2 | Feb 26, 2014 | Group: Database references |
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Revision 1.3 | Feb 28, 2024 | Group: Data collection / Database references / Derived calculations Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / 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_seq_id / _pdbx_struct_conn_angle.ptnr3_auth_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 |
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