登録情報 | データベース: PDB / ID: 4s10 |
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タイトル | Gelsolin nanobody shielding mutant plasma gelsolin from furin proteolysis |
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要素 | - GELSOLIN NANOBODY
- Gelsolin
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キーワード | METAL BINDING PROTEIN/IMMUNE SYSTEM / GELSOLIN-LIKE / ACTIN-BINDING / METAL BINDING PROTEIN-IMMUNE SYSTEM complex |
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機能・相同性 | 機能・相同性情報
striated muscle atrophy / regulation of establishment of T cell polarity / regulation of plasma membrane raft polarization / regulation of receptor clustering / renal protein absorption / positive regulation of keratinocyte apoptotic process / positive regulation of protein processing in phagocytic vesicle / positive regulation of actin nucleation / phosphatidylinositol 3-kinase catalytic subunit binding / actin cap ...striated muscle atrophy / regulation of establishment of T cell polarity / regulation of plasma membrane raft polarization / regulation of receptor clustering / renal protein absorption / positive regulation of keratinocyte apoptotic process / positive regulation of protein processing in phagocytic vesicle / positive regulation of actin nucleation / phosphatidylinositol 3-kinase catalytic subunit binding / actin cap / regulation of podosome assembly / myosin II binding / host-mediated suppression of symbiont invasion / actin filament severing / barbed-end actin filament capping / actin filament capping / actin filament depolymerization / cell projection assembly / actin polymerization or depolymerization / cardiac muscle cell contraction / Sensory processing of sound by outer hair cells of the cochlea / relaxation of cardiac muscle / podosome / phagocytosis, engulfment / cortical actin cytoskeleton / hepatocyte apoptotic process / cilium assembly / sarcoplasm / Caspase-mediated cleavage of cytoskeletal proteins / phagocytic vesicle / response to muscle stretch / phosphatidylinositol-4,5-bisphosphate binding / actin filament polymerization / actin filament organization / central nervous system development / protein destabilization / cellular response to type II interferon / actin filament binding / actin cytoskeleton / lamellipodium / actin binding / blood microparticle / secretory granule lumen / amyloid fibril formation / ficolin-1-rich granule lumen / Amyloid fiber formation / focal adhesion / calcium ion binding / Neutrophil degranulation / positive regulation of gene expression / extracellular space / extracellular exosome / extracellular region / plasma membrane / cytosol / cytoplasm類似検索 - 分子機能 Villin/Gelsolin / Gelsolin homology domain / Severin / Severin / Gelsolin-like domain / Gelsolin repeat / ADF-H/Gelsolin-like domain superfamily / Immunoglobulins / Immunoglobulin-like / Sandwich ...Villin/Gelsolin / Gelsolin homology domain / Severin / Severin / Gelsolin-like domain / Gelsolin repeat / ADF-H/Gelsolin-like domain superfamily / Immunoglobulins / Immunoglobulin-like / Sandwich / 3-Layer(aba) Sandwich / Mainly Beta / Alpha Beta類似検索 - ドメイン・相同性 |
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生物種 |  Lama glama (ラマ)
Homo sapiens (ヒト) |
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手法 | X線回折 / シンクロトロン / 分子置換 / 解像度: 2.614 Å |
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データ登録者 | Wongsantichon, J. / Robinson, R.C. / Gettemans, J. |
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引用 | ジャーナル: Hum.Mol.Genet. / 年: 2015 タイトル: An ER-directed gelsolin nanobody targets the first step in amyloid formation in a gelsolin amyloidosis mouse model. 著者: Van Overbeke, W. / Wongsantichon, J. / Everaert, I. / Verhelle, A. / Zwaenepoel, O. / Loonchanta, A. / Burtnick, L.D. / De Ganck, A. / Hochepied, T. / Haigh, J. / Cuvelier, C. / Derave, W. / ...著者: Van Overbeke, W. / Wongsantichon, J. / Everaert, I. / Verhelle, A. / Zwaenepoel, O. / Loonchanta, A. / Burtnick, L.D. / De Ganck, A. / Hochepied, T. / Haigh, J. / Cuvelier, C. / Derave, W. / Robinson, R.C. / Gettemans, J. |
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履歴 | 登録 | 2015年1月7日 | 登録サイト: RCSB / 処理サイト: RCSB |
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改定 1.0 | 2015年6月3日 | Provider: repository / タイプ: Initial release |
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改定 1.1 | 2024年11月20日 | Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Structure summary カテゴリ: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_entry_details / pdbx_modification_feature / 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_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_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_label_asym_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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