2PN5

Crystal Structure of TEP1r

2PN5 の概要

• エントリーDOI: 10.2210/pdb2pn5/pdb
• 分子名称: Thioester-containing protein I, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
• 機能のキーワード: full-length mature peptide, immune system
• 由来する生物種: Anopheles gambiae (African malaria mosquito)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 151689.51

構造登録者

Baxter, R.H.G. (登録日: 2007-04-23, 公開日: 2007-07-24, 最終更新日: 2024-10-30)

主引用文献

Baxter, R.H.G.,Chang, C.I.,Chelliah, Y.,Blandin, S.,Levashina, E.A.,Deisenhofer, J.
Structural basis for conserved complement factor-like function in the antimalarial protein TEP1
Proc.Natl.Acad.Sci.Usa, 104:11615-11620, 2007

PubMed Abstract: Thioester-containing proteins (TEPs) are a major component of the innate immune response of insects to invasion by bacteria and protozoa. TEPs form a distinct clade of a superfamily that includes the pan-protease inhibitors alpha(2)-macroglobulins and vertebrate complement factors. The essential feature of these proteins is a sequestered thioester bond that, after cleavage in a protease-sensitive region of the protein, is activated and covalently binds to its target. Recently, TEP1 from the malarial vector Anopheles gambiae was shown to mediate recognition and killing of ookinetes from the malarial parasite Plasmodium berghei, a model for the human malarial parasite Plasmodium falciparum. Here, we present the crystal structure of the TEP1 isoform TEP1r. Although the overall protein fold of TEP1r resembles that of complement factor C3, the TEP1r domains are repositioned to stabilize the inactive conformation of the molecule (containing an intact thioester) in the absence of the anaphylotoxin domain, a central component of complement factors. The structure of TEP1r provides a molecular basis for the differences between TEP1 alleles TEP1r and TEP1s, which correlate with resistance of A. gambiae to infection by P. berghei.

PubMed: 17606907
DOI: 10.1073/pnas.0704967104

実験手法

X-RAY DIFFRACTION (2.698 Å)