登録情報 | データベース: PDB / ID: 1ncj |
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タイトル | N-CADHERIN, TWO-DOMAIN FRAGMENT |
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要素 | PROTEIN (N-CADHERIN) |
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キーワード | CELL ADHESION PROTEIN |
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機能・相同性 | 機能・相同性情報
mesenchymal cell migration / regulation of oligodendrocyte progenitor proliferation / radial glial cell differentiation / neuroligin clustering involved in postsynaptic membrane assembly / regulation of postsynaptic density protein 95 clustering / positive regulation of synaptic vesicle clustering / Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) / Post-translational protein phosphorylation / Adherens junctions interactions / gamma-catenin binding ...mesenchymal cell migration / regulation of oligodendrocyte progenitor proliferation / radial glial cell differentiation / neuroligin clustering involved in postsynaptic membrane assembly / regulation of postsynaptic density protein 95 clustering / positive regulation of synaptic vesicle clustering / Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) / Post-translational protein phosphorylation / Adherens junctions interactions / gamma-catenin binding / synaptic vesicle clustering / desmosome / neural crest cell development / neuroepithelial cell differentiation / type B pancreatic cell development / fascia adherens / telencephalon development / neuronal stem cell population maintenance / alpha-catenin binding / calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules / apicolateral plasma membrane / Myogenesis / glial cell differentiation / cell-cell adhesion mediated by cadherin / catenin complex / brain morphogenesis / cell-cell junction assembly / blood vessel morphogenesis / heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules / cortical actin cytoskeleton / homophilic cell adhesion via plasma membrane adhesion molecules / plasma membrane raft / intercalated disc / homeostasis of number of cells / striated muscle cell differentiation / protein localization to plasma membrane / adherens junction / negative regulation of canonical Wnt signaling pathway / cell-cell adhesion / sarcolemma / beta-catenin binding / cerebral cortex development / cell-cell junction / cell migration / presynapse / lamellipodium / protein phosphatase binding / basolateral plasma membrane / cell adhesion / positive regulation of MAPK cascade / apical plasma membrane / synapse / calcium ion binding / protein kinase binding / enzyme binding / cell surface / RNA binding / identical protein binding / membrane / plasma membrane類似検索 - 分子機能 Cadherin prodomain like / Cadherin prodomain / Cadherin prodomain like / Cadherin, Y-type LIR-motif / Cadherin, Y-type LIR-motif / Cadherin / Catenin binding domain superfamily / Cadherins / Cadherin conserved site / Cadherin domain signature. ...Cadherin prodomain like / Cadherin prodomain / Cadherin prodomain like / Cadherin, Y-type LIR-motif / Cadherin, Y-type LIR-motif / Cadherin / Catenin binding domain superfamily / Cadherins / Cadherin conserved site / Cadherin domain signature. / Cadherin repeats. / Cadherin domain / Cadherin-like / Cadherins domain profile. / Cadherin-like superfamily / Immunoglobulin-like / Sandwich / Mainly Beta類似検索 - ドメイン・相同性 |
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生物種 |  Mus musculus (ハツカネズミ) |
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手法 | X線回折 / シンクロトロン / 分子置換 / 解像度: 3.4 Å |
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データ登録者 | Tamura, K. / Shan, W.-S. / Hendrickson, W.A. / Colman, D.R. / Shapiro, L. |
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引用 | ジャーナル: Neuron / 年: 1998 タイトル: Structure-function analysis of cell adhesion by neural (N-) cadherin. 著者: Tamura, K. / Shan, W.S. / Hendrickson, W.A. / Colman, D.R. / Shapiro, L. |
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履歴 | 登録 | 1999年2月2日 | 登録サイト: BNL / 処理サイト: RCSB |
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改定 1.0 | 1999年3月18日 | Provider: repository / タイプ: Initial release |
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改定 1.1 | 2008年4月26日 | Group: Version format compliance |
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改定 1.2 | 2011年7月13日 | Group: Version format compliance |
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改定 1.3 | 2023年8月16日 | Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description カテゴリ: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / 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.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_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_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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