5TVD

Crystal structure of Tm16

5TVD の概要

• エントリーDOI: 10.2210/pdb5tvd/pdb
• 分子名称: Tm16 (2 entities in total)
• 機能のキーワード: phosphatidylethanolamine-binding protein, unknown function
• 由来する生物種: Trichuris muris (Mouse whipworm)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 21371.85

構造登録者

Asojo, O.A. (登録日: 2016-11-08, 公開日: 2017-08-30, 最終更新日: 2023-10-04)

主引用文献

Liu, Z.,Kelleher, A.,Tabb, S.,Wei, J.,Pollet, J.,Hotez, P.J.,Bottazzi, M.E.,Zhan, B.,Asojo, O.A.
Identification, Characterization, and Structure of Tm16 from Trichuris muris.
J Parasitol Res, 2017:4342789-4342789, 2017

PubMed Abstract: Trichuriasis is a disease of poverty for which excretory and secretory (ES) products that induce the protective immunity are being investigated as candidate vaccines antigens. In this study, ES products of and immune sera were produced. The immune sera recognized more than 20 proteins on a 2D-gel of ES products of adult worms. Tm16 was one of the proteins identified by mass spectrometry. Tm16 shares 57% sequence identity with Ov16, an immunodominant diagnostic antigen from . Recombinant Tm16 with a carboxyl terminal hexahistidine was produced using Polyclonal antibodies against rTm16 were generated by one-prime and two-boost immunization of three female Balb/c mice with 25 g of recombinant Tm16 emulsified with ISA720 adjuvant. These polyclonal antibodies confirmed that Tm16 is localized to the ES products and the soluble fraction of the adult worm. Additionally, the high-resolution crystal structure of Tm16 was solved by molecular replacement. Tm16 belongs to the phosphatidylethanolamine-binding-like protein (PEBP1) family and this is the first structure of a PEBP1 from a parasite.

PubMed: 28884022
DOI: 10.1155/2017/4342789

実験手法

X-RAY DIFFRACTION (1.734 Å)