- EMDB-13794: Cryo-EM of the complex between human uromodulin (UMOD)/Tamm-Horsf... -
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基本情報
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データベース: EMDB / ID: EMD-13794
タイトル
Cryo-EM of the complex between human uromodulin (UMOD)/Tamm-Horsfall protein (THP) and the FimH lectin domain from uropathogenic E. coli
マップデータ
Unprocessed cryo-EM map of the lectin domain of fimbrial adhesin FimH from uropathogenic Escherichia coli bound to the branch of native human uromodulin (UMOD)/Tamm-Horsfall protein (THP).
試料
複合体: Complex of human uromodulin (UMOD)/Tamm-Horsfall protein (THP) and the lectin domain of the FimH adhesin of uropathogenic E. coli
複合体: Uromodulin
タンパク質・ペプチド: Uromodulin
複合体: Type 1 fimbiral adhesin FimH
タンパク質・ペプチド: Type 1 fimbiral adhesin FimH
機能・相同性
機能・相同性情報
citric acid secretion / metanephric thick ascending limb development / metanephric distal convoluted tubule development / connective tissue replacement / urea transmembrane transport / protein transport into plasma membrane raft / Asparagine N-linked glycosylation / micturition / organ or tissue specific immune response / metanephric ascending thin limb development ...citric acid secretion / metanephric thick ascending limb development / metanephric distal convoluted tubule development / connective tissue replacement / urea transmembrane transport / protein transport into plasma membrane raft / Asparagine N-linked glycosylation / micturition / organ or tissue specific immune response / metanephric ascending thin limb development / urate transport / collecting duct development / renal urate salt excretion / regulation of protein transport / protein localization to vacuole / antibacterial innate immune response / intracellular chloride ion homeostasis / renal sodium ion absorption / juxtaglomerular apparatus development / glomerular filtration / intracellular phosphate ion homeostasis / neutrophil migration / response to water deprivation / potassium ion homeostasis / cell adhesion involved in single-species biofilm formation / intracellular sodium ion homeostasis / regulation of urine volume / endoplasmic reticulum organization / renal water homeostasis / IgG binding / pilus / ciliary membrane / heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules / leukocyte cell-cell adhesion / extrinsic component of membrane / cellular response to unfolded protein / cellular defense response / multicellular organismal response to stress / side of membrane / chaperone-mediated protein folding / ERAD pathway / tumor necrosis factor-mediated signaling pathway / RNA splicing / apoptotic signaling pathway / lipid metabolic process / autophagy / cilium / regulation of blood pressure / spindle pole / intracellular calcium ion homeostasis / Golgi lumen / basolateral plasma membrane / defense response to Gram-negative bacterium / response to lipopolysaccharide / response to xenobiotic stimulus / inflammatory response / apical plasma membrane / negative regulation of cell population proliferation / calcium ion binding / cell surface / endoplasmic reticulum / extracellular space / extracellular exosome / membrane 類似検索 - 分子機能
ジャーナル: Nature / 年: 2021 タイトル: Highly accurate protein structure prediction with AlphaFold. 著者: John Jumper / Richard Evans / Alexander Pritzel / Tim Green / Michael Figurnov / Olaf Ronneberger / Kathryn Tunyasuvunakool / Russ Bates / Augustin Žídek / Anna Potapenko / Alex Bridgland / ...著者: John Jumper / Richard Evans / Alexander Pritzel / Tim Green / Michael Figurnov / Olaf Ronneberger / Kathryn Tunyasuvunakool / Russ Bates / Augustin Žídek / Anna Potapenko / Alex Bridgland / Clemens Meyer / Simon A A Kohl / Andrew J Ballard / Andrew Cowie / Bernardino Romera-Paredes / Stanislav Nikolov / Rishub Jain / Jonas Adler / Trevor Back / Stig Petersen / David Reiman / Ellen Clancy / Michal Zielinski / Martin Steinegger / Michalina Pacholska / Tamas Berghammer / Sebastian Bodenstein / David Silver / Oriol Vinyals / Andrew W Senior / Koray Kavukcuoglu / Pushmeet Kohli / Demis Hassabis / 要旨: Proteins are essential to life, and understanding their structure can facilitate a mechanistic understanding of their function. Through an enormous experimental effort, the structures of around ...Proteins are essential to life, and understanding their structure can facilitate a mechanistic understanding of their function. Through an enormous experimental effort, the structures of around 100,000 unique proteins have been determined, but this represents a small fraction of the billions of known protein sequences. Structural coverage is bottlenecked by the months to years of painstaking effort required to determine a single protein structure. Accurate computational approaches are needed to address this gap and to enable large-scale structural bioinformatics. Predicting the three-dimensional structure that a protein will adopt based solely on its amino acid sequence-the structure prediction component of the 'protein folding problem'-has been an important open research problem for more than 50 years. Despite recent progress, existing methods fall far short of atomic accuracy, especially when no homologous structure is available. Here we provide the first computational method that can regularly predict protein structures with atomic accuracy even in cases in which no similar structure is known. We validated an entirely redesigned version of our neural network-based model, AlphaFold, in the challenging 14th Critical Assessment of protein Structure Prediction (CASP14), demonstrating accuracy competitive with experimental structures in a majority of cases and greatly outperforming other methods. Underpinning the latest version of AlphaFold is a novel machine learning approach that incorporates physical and biological knowledge about protein structure, leveraging multi-sequence alignments, into the design of the deep learning algorithm.
ダウンロード / ファイル: emd_13794.map.gz / 形式: CCP4 / 大きさ: 244.1 MB / タイプ: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
注釈
Unprocessed cryo-EM map of the lectin domain of fimbrial adhesin FimH from uropathogenic Escherichia coli bound to the branch of native human uromodulin (UMOD)/Tamm-Horsfall protein (THP).
Cryo-EM half map 2 of the lectin domain of fimbrial adhesin FimH from uropathogenic Escherichia coli bound to the branch of native human uromodulin (UMOD)/Tamm-Horsfall protein (THP).
Cryo-EM half map 1 of the lectin domain of fimbrial adhesin FimH from uropathogenic Escherichia coli bound to the branch of native human uromodulin (UMOD)/Tamm-Horsfall protein (THP).
全体 : Complex of human uromodulin (UMOD)/Tamm-Horsfall protein (THP) an...
全体
名称: Complex of human uromodulin (UMOD)/Tamm-Horsfall protein (THP) and the lectin domain of the FimH adhesin of uropathogenic E. coli
要素
複合体: Complex of human uromodulin (UMOD)/Tamm-Horsfall protein (THP) and the lectin domain of the FimH adhesin of uropathogenic E. coli
複合体: Uromodulin
タンパク質・ペプチド: Uromodulin
複合体: Type 1 fimbiral adhesin FimH
タンパク質・ペプチド: Type 1 fimbiral adhesin FimH
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超分子 #1: Complex of human uromodulin (UMOD)/Tamm-Horsfall protein (THP) an...
超分子
名称: Complex of human uromodulin (UMOD)/Tamm-Horsfall protein (THP) and the lectin domain of the FimH adhesin of uropathogenic E. coli タイプ: complex / ID: 1 / 親要素: 0 / 含まれる分子: all