3K60

Crystal structure of N-terminal domain of Plasmodium falciparum Hsp90 (PF07_0029) bound to ADP

3K60 の概要

• エントリーDOI: 10.2210/pdb3k60/pdb
• 関連するPDBエントリー: 1Y6Z 3IED
• 分子名称: Heat shock protein 86, ADENOSINE-5'-DIPHOSPHATE, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: chaperone, atpase, stress response
• 由来する生物種: Plasmodium falciparum; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 51480.37

構造登録者

Corbett, K.D.,Berger, J.M. (登録日: 2009-10-08, 公開日: 2010-08-18, 最終更新日: 2023-09-06)

主引用文献

Corbett, K.D.,Berger, J.M.
Structure of the ATP-binding domain of Plasmodium falciparum Hsp90.
Proteins, 78:2738-2744, 2010

PubMed Abstract: Hsp90 is an important cellular chaperone and attractive target for therapeutics against both cancer and infectious organisms. The Hsp90 protein from the parasite Plasmodium falciparum, the causative agent of malaria, is critical for this organism's survival; the anti-Hsp90 drug geldanamycin is toxic to P. falciparum growth. We have solved the structure of the N-terminal ATP-binding domain of P. falciparum Hsp90, which contains a principal drug-binding pocket, in both apo and ADP-bound states at 2.3 A resolution. The structure shows that P. falciparum Hsp90 is highly similar to human Hsp90, and likely binds agents such as geldanamycin in an identical manner. Our results should aid in the structural understanding of Hsp90-drug interactions in P. falciparum, and provide a scaffold for future drug-discovery efforts.

PubMed: 20635416
DOI: 10.1002/prot.22799

実験手法

X-RAY DIFFRACTION (2.3 Å)