Crystal structure of the FYCO1 RUN domain suggests possible interfaces with small GTPases

• 資料種別: 記事
• タイトル: Crystal structure of the FYCO1 RUN domain suggests possible interfaces with small GTPases
• 著者標目: Shunya Sakurai; Toshiyuki Shimizu; Umeharu Ohto
• 出版年月日等: 2020-07-28
• 出版年（W3CDTF）: 2020-07-28
• タイトル（掲載誌）: Acta Crystallographica Section F Structural Biology Communications
• 巻号年月日等（掲載誌）: 76 8
• 掲載巻: 76
• 掲載号: 8
• 掲載ページ: 326-333
• 掲載年月日（W3CDTF）: 2020-07-28
• 出版事項（掲載誌）: International Union of Crystallography (IUCr)
• 件名標目: Protein Conformation, alpha-Helical; Genetic Vectors; Gene Expression; Crystallography, X-Ray; Escherichia coli; Animals; Guanine Nucleotide Exchange Factors; Humans; Protein Interaction Domains and Motifs; Amino Acid Sequence; Cloning, Molecular; Adaptor Proteins, Signal Transducing; Binding Sites; Sequence Homology, Amino Acid; Recombinant Proteins; Molecular Docking Simulation; Cytoskeletal Proteins; Protein Conformation, beta-Strand; Carrier Proteins; Microtubule-Associated Proteins; Sequence Alignment; Protein Binding
• 対象利用者: 一般
• 標準番号（その他）: PMID : 32744243
• DOI: 10.1107/s2053230x20009012; https://doi.org/10.1107/s2053230x20009012
• 作成日（W3CDTF）: 2020-07-28
• 著作権情報: http://journals.iucr.org/services/copyrightpolicy.html; http://journals.iucr.org/services/copyrightpolicy.html#TDM
• 関連情報（URI）: http://journals.iucr.org/f/issues/2020/08/00/tb5160/tb5160.pdf
• 参照: Accelerating Protein Docking in ZDOCK Using an Advanced 3D Convolution Library; https://cir.nii.ac.jp/crid/1360011144003705600; Crystal Structure of the RUN Domain of the RAP2-interacting Protein x; https://cir.nii.ac.jp/crid/1360011144468337152; <i>PHENIX</i>: building new software for automated crystallographic structure determination; https://cir.nii.ac.jp/crid/1360011145213187328; Autophagy and human diseases; https://cir.nii.ac.jp/crid/1360283691765128448; The crystal structure of mouse LC3B in complex with the FYCO1 LIR reveals the importance of the flanking region of the LIR motif; https://cir.nii.ac.jp/crid/1360285710063240704; <i>MolProbity</i>: all-atom structure validation for macromolecular crystallography; https://cir.nii.ac.jp/crid/1360292617908937344; [20] Processing of X-ray diffraction data collected in oscillation mode; https://cir.nii.ac.jp/crid/1360292619971626752; Structural Basis for Recruitment of Rab6-Interacting Protein 1 to Golgi via a RUN Domain; https://cir.nii.ac.jp/crid/1360574096431507072; Autophagy: Renovation of Cells and Tissues; https://cir.nii.ac.jp/crid/1360846640782439680; Rab35/ACAP2 and Rab35/RUSC2 Complex Structures Reveal Molecular Basis for Effector Recognition by Rab35 GTPase; https://cir.nii.ac.jp/crid/1360855568470214144; FYCO1 Contains a C-terminally Extended, LC3A/B-preferring LC3-interacting Region (LIR) Motif Required for Efficient Maturation of Autophagosomes during Basal Autophagy; https://cir.nii.ac.jp/crid/1360855569270039168; Autophagy: process and function; https://cir.nii.ac.jp/crid/1361137044013333120; The LIR motif – crucial for selective autophagy; https://cir.nii.ac.jp/crid/1361137045752944896; The crystal structure of human rac1, a member of the rho-family complexed with a GTP analogue; https://cir.nii.ac.jp/crid/1361418518624772736; Structural basis of FYCO1 and MAP1LC3A interaction reveals a novel binding mode for Atg8-family proteins; https://cir.nii.ac.jp/crid/1362262943984841344; Crystal structures of the small G protein Rap2A in complex with its substrate GTP, with GDP and with GTPgamma S; https://cir.nii.ac.jp/crid/1362262944136474240; Structure-based development of new RAS-effector inhibitors from a combination of active and inactive RAS-binding compounds; https://cir.nii.ac.jp/crid/1362262944297091456; Autophagy and microtubules – new story, old players; https://cir.nii.ac.jp/crid/1362544418589623552; Molecular replacement with<i>MOLREP</i>; https://cir.nii.ac.jp/crid/1362544420617100928; Structural basis of family-wide Rab GTPase recognition by rabenosyn-5; https://cir.nii.ac.jp/crid/1362544420951717376; Hyperthermophile genome; https://cir.nii.ac.jp/crid/1362544421354356352; The structural GDP/GTP cycle of human Arf6; https://cir.nii.ac.jp/crid/1363107368565584128; Features and development of <i>Coot</i>; https://cir.nii.ac.jp/crid/1363107370089014528; The pre-hydrolysis state of p21ras in complex with GTP: new insights into the role of water molecules in the GTP hydrolysis reaction of ras-like proteins; https://cir.nii.ac.jp/crid/1363107370833002240; Autophagy as a Regulated Pathway of Cellular Degradation; https://cir.nii.ac.jp/crid/1363388843355995008; FYCO1 is a Rab7 effector that binds to LC3 and PI3P to mediate microtubule plus end–directed vesicle transport; https://cir.nii.ac.jp/crid/1363388843724543616; FYVE fingers bind PtdIns(3)P; https://cir.nii.ac.jp/crid/1363670319903763200; Crystal Structure of Human RhoA in a Dominantly Active Form Complexed with a GTP Analogue; https://cir.nii.ac.jp/crid/1363951795100435072; Structural basis for recruitment of RILP by small GTPase Rab7; https://cir.nii.ac.jp/crid/1363951796118755456; Crystal structure and functional implication of the RUN domain of human NESCA; https://cir.nii.ac.jp/crid/1364233268885689600; <i>REFMAC</i>5 for the refinement of macromolecular crystal structures; https://cir.nii.ac.jp/crid/1364233269451938048; RUN domains: a new family of domains involved in Ras-like GTPase signaling; https://cir.nii.ac.jp/crid/1364233269818995968; Genome-wide Investigation of the Rab Binding Activity of RUN Domains: Development of a Novel Tool that Specifically Traps GTP-Rab35; https://cir.nii.ac.jp/crid/1390282679673511424
• 連携機関・データベース: 国立情報学研究所 : CiNii Research; https://cir.nii.ac.jp/
• 提供元機関・データベース: Crossref; https://www.crossref.org; 科学研究費助成事業データベース; https://kaken.nii.ac.jp/ja

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