2BIT

Crystal structure of human cyclophilin D at 1.7 A resolution

2BIT の概要

• エントリーDOI: 10.2210/pdb2bit/pdb
• 関連するPDBエントリー: 2BIU
• 分子名称: PEPTIDYL-PROLYL CIS-TRANS ISOMERASE (2 entities in total)
• 機能のキーワード: crystal engineering, cis-tran-isomerization, human, mitochondrial protein, isomerase
• 由来する生物種: HOMO SAPIENS (HUMAN)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17739.21

構造登録者

Hennig, M.,Thoma, R.,Stihle, M.,Schlatter, D. (登録日: 2005-01-26, 公開日: 2005-01-26, 最終更新日: 2023-12-13)

主引用文献

Schlatter, D.,Thoma, R.,Kueng, E.,Stihle, M.,Mueller, F.,Boroni, E.,Hennig, M.
Crystal Engineering Yields Crystals of Cyclophilin D Diffracting to 1.7 A Resolution
Acta Crystallogr.,Sect.D, 61:513-519, 2005

PubMed Abstract: In the pharmaceutical industry, knowledge of the three-dimensional structure of a specific target facilitates the drug-discovery process. Despite possessing favoured analytical properties such as high purity and monodispersion in light scattering, some proteins are not capable of forming crystals suitable for X-ray analysis. Cyclophilin D, an isoform of cyclophilin that is expressed in the mitochondria, was selected as a drug target for the treatment of cardiac disorders. As the wild-type enzyme defied all attempts at crystallization, protein engineering on the enzyme surface was performed. The K133I mutant gave crystals that diffracted to 1.7 A resolution using in-house X-ray facilities and were suitable for soaking experiments. The crystals were very robust and diffraction was maintained after soaking in 25% DMSO solution: excellent conditions for the rapid analysis of complex structures including crystallographic fragment screening.

PubMed: 15858260
DOI: 10.1107/S0907444905003070

実験手法

X-RAY DIFFRACTION (1.71 Å)