6OYB

Crystal structure of H62G mutant of human macrophage migration inhibitory factor

6OYB の概要

• エントリーDOI: 10.2210/pdb6oyb/pdb
• 分子名称: Macrophage migration inhibitory factor, SULFATE ION, GLYCEROL, ... (5 entities in total)
• 機能のキーワード: isomerase, trimeric, mutation
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 37786.80

構造登録者

Pantouris, G.,Lolis, E. (登録日: 2019-05-14, 公開日: 2020-04-22, 最終更新日: 2023-10-11)

主引用文献

Pantouris, G.,Khurana, L.,Ma, A.,Skeens, E.,Reiss, K.,Batista, V.S.,Lisi, G.P.,Lolis, E.J.
Regulation of MIF Enzymatic Activity by an Allosteric Site at the Central Solvent Channel.
Cell Chem Biol, 27:740-750.e5, 2020

PubMed Abstract: In proteins with multiple functions, such as macrophage migration inhibitory factor (MIF), the study of its intramolecular dynamic network can offer a unique opportunity to understand how a single protein is able to carry out several nonoverlapping functions. A dynamic mechanism that controls the MIF-induced activation of CD74 was recently discovered. In this study, the regulation of tautomerase activity was explored. The catalytic base Pro1 is found to form dynamic communications with the same allosteric node that regulates CD74 activation. Signal transmission between the allosteric and catalytic sites take place through intramolecular aromatic interactions and a hydrogen bond network that involves residues and water molecules of the MIF solvent channel. Once thought to be a consequence of trimerization, a regulatory function for the solvent channel is now defined. These results provide mechanistic insights into the regulation of catalytic activity and the role of solvent channel water molecules in MIF catalysis.

PubMed: 32433911
DOI: 10.1016/j.chembiol.2020.05.001

実験手法

X-RAY DIFFRACTION (1.53 Å)