登録情報 データベース : PDB / ID : 4fe8 構造の表示 ダウンロードとリンクタイトル Crystal Structure of Htt36Q3H-EX1-X1-C1(Alpha) 要素Maltose-binding periplasmic protein,Huntingtin 詳細 キーワード SIGNALING PROTEIN / alpha helix / loop / beta-strand hairpin / Beta strand hairpin / Disease protein機能・相同性 機能・相同性情報分子機能 ドメイン・相同性 構成要素
regulation of cAMP-dependent protein kinase activity / regulation of phosphoprotein phosphatase activity / positive regulation of inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity / microtubule-based transport / vocal learning / regulation of CAMKK-AMPK signaling cascade / positive regulation of mitophagy / profilin binding / vesicle transport along microtubule / positive regulation of cilium assembly ... regulation of cAMP-dependent protein kinase activity / regulation of phosphoprotein phosphatase activity / positive regulation of inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity / microtubule-based transport / vocal learning / regulation of CAMKK-AMPK signaling cascade / positive regulation of mitophagy / profilin binding / vesicle transport along microtubule / positive regulation of cilium assembly / presynaptic cytosol / retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum / positive regulation of aggrephagy / postsynaptic cytosol / positive regulation of lipophagy / dynein intermediate chain binding / detection of maltose stimulus / maltose transport complex / beta-tubulin binding / Golgi organization / carbohydrate transport / establishment of mitotic spindle orientation / dynactin binding / Regulation of MECP2 expression and activity / carbohydrate transmembrane transporter activity / maltose binding / maltose transport / maltodextrin transmembrane transport / autophagosome / ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing / inclusion body / heat shock protein binding / centriole / ATP-binding cassette (ABC) transporter complex / cell chemotaxis / negative regulation of extrinsic apoptotic signaling pathway / protein destabilization / cytoplasmic vesicle membrane / kinase binding / p53 binding / late endosome / outer membrane-bounded periplasmic space / transmembrane transporter binding / periplasmic space / early endosome / positive regulation of apoptotic process / axon / apoptotic process / DNA damage response / dendrite / perinuclear region of cytoplasm / Golgi apparatus / endoplasmic reticulum / protein-containing complex / nucleoplasm / identical protein binding / membrane / nucleus / cytoplasm / cytosol 類似検索 - 分子機能 Huntingtin / Huntingtin, middle-repeat / Huntingtin family / : / : / : / Huntingtin, N-terminal HEAT / Huntingtin, bridge / Huntingtin, N-terminal HEAT 1 / Huntingtin, C-terminal HEAT ... Huntingtin / Huntingtin, middle-repeat / Huntingtin family / : / : / : / Huntingtin, N-terminal HEAT / Huntingtin, bridge / Huntingtin, N-terminal HEAT 1 / Huntingtin, C-terminal HEAT / Maltose/Cyclodextrin ABC transporter, substrate-binding protein / Solute-binding family 1, conserved site / Bacterial extracellular solute-binding proteins, family 1 signature. / Bacterial extracellular solute-binding protein / Bacterial extracellular solute-binding protein / Periplasmic binding protein-like II / D-Maltodextrin-Binding Protein; domain 2 / Armadillo-like helical / Armadillo-type fold / 3-Layer(aba) Sandwich / Alpha Beta 類似検索 - ドメイン・相同性 Maltose/maltodextrin-binding periplasmic protein / Huntingtin 類似検索 - 構成要素生物種 Escherichia coli (大腸菌)Homo sapiens (ヒト)手法 X線回折 / シンクロトロン / 分子置換 / 解像度 : 3 Å 詳細データ登録者 Kim, M. 引用ジャーナル : Prion / 年 : 2013タイトル : Beta conformation of polyglutamine track revealed by a crystal structure of Huntingtin N-terminal region with insertion of three histidine residues.著者 : Kim, M. 履歴 登録 2012年5月29日 登録サイト : RCSB / 処理サイト : RCSB改定 1.0 2013年3月13日 Provider : repository / タイプ : Initial release改定 1.1 2013年7月3日 Group : Database references改定 1.2 2017年6月14日 Group : Database references / Source and taxonomy / Structure summaryカテゴリ : citation / entity ... citation / entity / entity_name_com / entity_src_gen / struct_ref_seq_dif Item : _citation.journal_id_CSD / _citation.journal_id_ISSN ... _citation.journal_id_CSD / _citation.journal_id_ISSN / _entity.pdbx_description / _entity.pdbx_fragment / _entity.pdbx_mutation / _entity_name_com.name / _struct_ref_seq_dif.align_id / _struct_ref_seq_dif.details / _struct_ref_seq_dif.pdbx_seq_db_accession_code 改定 1.3 2024年2月28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 / 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 / _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_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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