4ANP

Crystal structure of human phenylalanine hydroxylase in complex with a pharmacological chaperone

4ANP の概要

• エントリーDOI: 10.2210/pdb4anp/pdb
• 関連するPDBエントリー: 1DMW 1J8T 1J8U 1KW0 1LRM 1MMK 1MMT 1PAH 1TDW 1TG2 2PAH 3PAH 4PAH 5PAH 6PAH
• 分子名称: PHENYLALANINE-4-HYDROXYLASE, FE (III) ION, 5,6-DIMETHYL-3-(4-METHYL-2-PYRIDINYL)-2-THIOXO-2,3-DIHYDROTHIENO[2,3- D]PYRIMIDIN-4(1H)-ONE, ... (4 entities in total)
• 機能のキーワード: oxidoreductase, phenylketonuria, folding mechanism
• 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: 37903.77

構造登録者

Torreblanca, R.,Lira-Navarrete, E.,Sancho, J.,Hurtado-Guerrero, R. (登録日: 2012-03-21, 公開日: 2012-04-11, 最終更新日: 2023-12-20)

主引用文献

Torreblanca, R.,Lira-Navarrete, E.,Sancho, J.,Hurtado-Guerrero, R.
Structural and Mechanistic Basis of the Interaction between a Pharmacological Chaperone and Human Phenylalanine Hydroxylase.
Chembiochem, 13:1266-, 2012

PubMed Abstract: Not without a chaperone: Pharmacological chaperones are designed to bind and ideally stabilise their target protein. Here, we elucidate the molecular mechanism of a potential pharmacological chaperone to treat phenylketonuria. The crystal structure of human phenylalanine hydroxylase with compound IV may help in the rational design of more efficient compounds to treat this disease.

PubMed: 22549968
DOI: 10.1002/CBIC.201200188

実験手法

X-RAY DIFFRACTION (2.11 Å)