4F2K

Macrophage Migration Inhibitory Factor covalently complexed with phenethylisothiocyanate

4F2K の概要

• エントリーDOI: 10.2210/pdb4f2k/pdb
• 分子名称: Macrophage migration inhibitory factor, N-(2-phenylethyl)thioformamide, SULFATE ION, ... (5 entities in total)
• 機能のキーワード: cytokine, tautomerase, phenethylisothiocyanate, isomerase, isomerase-isomerase inhibitor complex, isomerase/isomerase inhibitor
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Secreted: P14174
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 38185.57

構造登録者

Tyndall, J.D.A.,Bernhagen, J.,Hampton, M.B.,Wilbanks, S.M.,Rutledge, M.T. (登録日: 2012-05-08, 公開日: 2012-06-06, 最終更新日: 2024-11-20)

主引用文献

Tyndall, J.D.A.,Lue, H.,Rutledge, M.T.,Bernhagen, J.,Hampton, M.B.,Wilbanks, S.M.
Macrophage migration inhibitory factor covalently complexed with phenethyl isothiocyanate
Acta Crystallogr.,Sect.F, 68:999-1002, 2012

PubMed Abstract: Macrophage migration inhibitory factor is irreversibly inhibited via covalent modification by phenethyl isothiocyanate, a naturally occurring compound with anti-inflammatory and anticancer properties. The structure of the modified protein obtained from X-ray diffraction data to 1.64 Å resolution is presented. The inhibitor sits within a deep hydrophobic pocket between subunits of the homotrimer and is highly ordered. The secondary structure of macrophage migratory inhibitory factor is unchanged by this modification, but there are significant rearrangements, including of the side-chain position of Tyr37 and the main chain of residues 31-34. These changes may explain the decreased binding of the modified protein to the receptor CD74. Together with the pocket, the areas of conformational change define specific targets for the design of more selective and potent inhibitors as potential therapeutics.

PubMed: 22949182
DOI: 10.1107/S1744309112030552

実験手法

X-RAY DIFFRACTION (1.53 Å)