1R19
 
 | | Crystal Structure Analysis of S.epidermidis adhesin SdrG binding to Fibrinogen (Apo structure) | | 分子名称: | fibrinogen-binding protein SdrG | | 著者 | Ponnuraj, K, Bowden, M.G, Davis, S, Gurusiddappa, S, Moore, D, Choe, D, Xu, Y, Hook, M, Narayana, S.V.L. | | 登録日 | 2003-09-23 | | 公開日 | 2003-10-28 | | 最終更新日 | 2023-08-23 | | 実験手法 | X-RAY DIFFRACTION (3.51 Å) | | 主引用文献 | A "dock, lock and latch" Structural Model for a Staphylococcal Adhesin Binding to Fibrinogen
Cell(Cambridge,Mass.), 115, 2003
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1R17
 | | Crystal Structure Analysis of S.epidermidis adhesin SdrG binding to Fibrinogen (adhesin-ligand complex) | | 分子名称: | CALCIUM ION, fibrinogen-binding protein SdrG, fibrinopeptide B | | 著者 | Ponnuraj, K, Bowden, M.G, Davis, S, Gurusiddappa, S, Moore, D, Choe, D, Xu, Y, Hook, M, Narayana, S.V.L. | | 登録日 | 2003-09-23 | | 公開日 | 2003-10-28 | | 最終更新日 | 2024-02-14 | | 実験手法 | X-RAY DIFFRACTION (1.86 Å) | | 主引用文献 | A "dock, lock and latch" Structural Model for a Staphylococcal Adhesin Binding to Fibrinogen
Cell(Cambridge,Mass.), 115, 2003
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2RAL
 | | Crystal Structure Analysis of double cysteine mutant of S.epidermidis adhesin SdrG: Evidence for the Dock,Lock and Latch ligand binding mechanism | | 分子名称: | Serine-aspartate repeat-containing protein G | | 著者 | Ponnuraj, K, Sthanam, N, Bowden, M.G, Hook, M. | | 登録日 | 2007-09-17 | | 公開日 | 2007-11-06 | | 最終更新日 | 2023-08-30 | | 実験手法 | X-RAY DIFFRACTION (2.8 Å) | | 主引用文献 | Evidence for the "dock, lock, and latch" ligand binding mechanism of the staphylococcal microbial surface component recognizing adhesive matrix molecules (MSCRAMM) SdrG.
J.Biol.Chem., 283, 2008
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8G21
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5OQV
 | | Near-atomic resolution fibril structure of complete amyloid-beta(1-42) by cryo-EM | | 分子名称: | Amyloid beta A4 protein | | 著者 | Gremer, L, Schoelzel, D, Schenk, C, Reinartz, E, Labahn, J, Ravelli, R, Tusche, M, Lopez-Iglesias, C, Hoyer, W, Heise, H, Willbold, D, Schroeder, G.F. | | 登録日 | 2017-08-14 | | 公開日 | 2017-09-13 | | 最終更新日 | 2024-05-15 | | 実験手法 | ELECTRON MICROSCOPY (4 Å) | | 主引用文献 | Fibril structure of amyloid-beta (1-42) by cryo-electron microscopy.
Science, 358, 2017
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