4TR9
Ternary co-crystal structure of fructose-bisphosphate aldolase from Plasmodium falciparum in complex with TRAP and a small molecule inhibitor
4TR9 の概要
| エントリーDOI | 10.2210/pdb4tr9/pdb |
| 関連するPDBエントリー | 2pc4 |
| 分子名称 | Fructose-bisphosphate aldolase, ALA-ALA-SER-LEU-TYR-GLU-LYS-LYS-ALA-ALA, ALA-ALA-ALA-SER-LEU-TYR-GLU-LYS-LYS-ALA-ALA, ... (6 entities in total) |
| 機能のキーワード | lyase-lyase inhibitor complex, lyase/lyase inhibitor |
| 由来する生物種 | Plasmodium falciparum 詳細 |
| タンパク質・核酸の鎖数 | 10 |
| 化学式量合計 | 165823.37 |
| 構造登録者 | |
| 主引用文献 | Nemetski, S.M.,Cardozo, T.J.,Bosch, G.,Weltzer, R.,O'Malley, K.,Ejigiri, I.,Kumar, K.A.,Buscaglia, C.A.,Nussenzweig, V.,Sinnis, P.,Levitskaya, J.,Bosch, J. Inhibition by stabilization: targeting the Plasmodium falciparum aldolase-TRAP complex. Malar.J., 14:324-324, 2015 Cited by PubMed Abstract: Emerging resistance of the malaria parasite Plasmodium to current therapies underscores the critical importance of exploring novel strategies for disease eradication. Plasmodium species are obligate intracellular protozoan parasites. They rely on an unusual form of substrate-dependent motility for their migration on and across host-cell membranes and for host cell invasion. This peculiar motility mechanism is driven by the 'glideosome', an actin-myosin associated, macromolecular complex anchored to the inner membrane complex of the parasite. Myosin A, actin, aldolase, and thrombospondin-related anonymous protein (TRAP) constitute the molecular core of the glideosome in the sporozoite, the mosquito stage that brings the infection into mammals. PubMed: 26289816DOI: 10.1186/s12936-015-0834-9 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.111 Å) |
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