4O8I

1.45A resolution structure of PEG 400 Bound Cyclophilin D

4O8I の概要

• エントリーDOI: 10.2210/pdb4o8i/pdb
• 関連するPDBエントリー: 4O8H
• 分子名称: Peptidyl-prolyl cis-trans isomerase F, mitochondrial, PENTAETHYLENE GLYCOL (3 entities in total)
• 機能のキーワード: isomerase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Mitochondrion matrix : P30405
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17977.48

構造登録者

Lovell, S.,Valasani, K.R.,Battaile, K.P.,Wang, C.,Yan, S.S. (登録日: 2013-12-27, 公開日: 2014-06-11, 最終更新日: 2023-09-20)

主引用文献

Valasani, K.R.,Carlson, E.A.,Battaile, K.P.,Bisson, A.,Wang, C.,Lovell, S.,ShiDu Yan, S.
High-resolution crystal structures of two crystal forms of human cyclophilin D in complex with PEG 400 molecules.
Acta Crystallogr F Struct Biol Commun, 70:717-722, 2014

PubMed Abstract: Cyclophilin D (CypD) is a key mitochondrial target for amyloid-β-induced mitochondrial and synaptic dysfunction and is considered a potential drug target for Alzheimer's disease. The high-resolution crystal structures of primitive orthorhombic (CypD-o) and primitive tetragonal (CypD-t) forms have been determined to 1.45 and 0.85 Å resolution, respectively, and are nearly identical structurally. Although an isomorphous structure of CypD-t has previously been reported, the structure reported here was determined at atomic resolution, while CypD-o represents a new crystal form for this protein. In addition, each crystal form contains a PEG 400 molecule bound to the same region along with a second PEG 400 site in CypD-t which occupies the cyclosporine A inhibitor binding site of CypD. Highly precise structural information for CypD should be extremely useful for discerning the detailed interaction of small molecules, particularly drugs and/or inhibitors, bound to CypD. The 0.85 Å resolution structure of CypD-t is the highest to date for any CypD structure.

PubMed: 24915078
DOI: 10.1107/S2053230X14009480

実験手法

X-RAY DIFFRACTION (1.45 Å)