3P3K

The crystal structure of translationally controlled tumor protein (TCTP) of Plasmodium falciparum

3P3K の概要

• エントリーDOI: 10.2210/pdb3p3k/pdb
• 関連するPDBエントリー: 1TXJ
• 分子名称: Translationally-controlled tumor protein homolog (2 entities in total)
• 機能のキーワード: mainly beta, metal binding protein
• 由来する生物種: Plasmodium falciparum
• 細胞内の位置: Cytoplasm (By similarity): Q8I3Z5
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 21638.19

構造登録者

Eichhorn, T.,Winter, D.,Dirdjaja, N.,Frank, M.,Krauth-Siegel, L.,Granzin, J.,Efferth, T. (登録日: 2010-10-05, 公開日: 2011-11-09, 最終更新日: 2023-09-06)

主引用文献

Eichhorn, T.,Winter, D.,Buchele, B.,Dirdjaja, N.,Frank, M.,Lehmann, W.D.,Mertens, R.,Krauth-Siegel, R.L.,Simmet, T.,Granzin, J.,Efferth, T.
Molecular interaction of artemisinin with translationally controlled tumor protein (TCTP) of Plasmodium falciparum.
Biochem Pharmacol, 85:38-45, 2013

PubMed Abstract: Malaria causes millions of death cases per year. Since Plasmodium falciparum rapidly develops drug resistance, it is of high importance to investigate potential drug targets which may lead to novel rational therapy approaches. Here we report on the interaction of translationally controlled tumor protein of P. falciparum (PfTCTP) with the anti-malarial drug artemisinin. Furthermore, we investigated the crystal structure of PfTCTP. Using mass spectrometry, bioinformatic approaches and surface plasmon resonance spectroscopy, we identified novel binding sites of artemisinin which are in direct neighborhood to amino acids 19-46, 108-134 and 140-163. The regions covered by these residues are known to be functionally important for TCTP function. We conclude that interaction of artemisinin with TCTP may be at least in part explain the antimalarial activity of artemisinin.

PubMed: 23085438
DOI: 10.1016/j.bcp.2012.10.006

実験手法

X-RAY DIFFRACTION (2.551 Å)