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8UR2

Crystal Structure of macrophage migration inhibitory factor (MIF) from Trichomonas vaginalis (I41 form)

8UR2 の概要
エントリーDOI10.2210/pdb8ur2/pdb
分子名称MACROPHAGE MIGRATION INHIBITORY FACTOR, IODIDE ION, PYRUVIC ACID, ... (4 entities in total)
機能のキーワードssgcid, structural genomics, seattle structural genomics center for infectious disease, macrophage migration inhibitory factor, cytokine
由来する生物種Trichomonas vaginalis G3
タンパク質・核酸の鎖数6
化学式量合計89271.75
構造登録者
主引用文献Srivastava, A.,Nair, A.,Dawson, O.C.O.,Gao, R.,Liu, L.,Craig, J.K.,Battaile, K.P.,Harmon, E.K.,Barrett, L.K.,Van Voorhis, W.C.,Subramanian, S.,Myler, P.J.,Lovell, S.,Asojo, O.A.,Darwiche, R.
Structures of Trichomonas vaginalis macrophage migratory inhibitory factor.
Acta Crystallogr.,Sect.F, 80:341-347, 2024
Cited by
PubMed Abstract: The unicellular parasitic protozoan Trichomonas vaginalis causes trichomoniasis, the most prevalent nonviral sexually transmitted disease globally. T. vaginalis evades host immune responses by producing homologs of host proteins, including cytokines such as macrophage migration inhibitory factor. T. vaginalis macrophage migration inhibitory factor (TvMIF) helps to facilitate the survival of T. vaginalis during nutritional stress conditions, increases prostate cell proliferation and invasiveness, and induces inflammation-related cellular pathways, thus mimicking the ability of human MIF to increase inflammation and cell proliferation. The production, crystallization and three structures of N-terminally hexahistidine-tagged TvMIF reveal a prototypical MIF trimer with a topology similar to that of human homologs (hMIF-1 and hMIF-2). The N-terminal tag obscures the expected pyruvate-binding site. The similarity of TvMIF to its human homologs can be exploited for structure-based drug discovery.
PubMed: 39601418
DOI: 10.1107/S2053230X24011105
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.9 Å)
構造検証レポート
Validation report summary of 8ur2
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-15に公開中

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