2OMV

Crystal structure of InlA S192N Y369S/hEC1 complex

2OMV の概要

• エントリーDOI: 10.2210/pdb2omv/pdb
• 分子名称: Internalin-A, Epithelial-cadherin, CALCIUM ION, ... (5 entities in total)
• 機能のキーワード: leucine-rich-repeat, invasion protein, ig-like domain, adhesion protein, cell invasion-cell adhesion complex, cell invasion/cell adhesion
• 由来する生物種: Listeria monocytogenes; 詳細
• 細胞内の位置: Cell junction : P12830
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 61452.68

構造登録者

Wollert, T.,Heinz, D.W.,Schubert, W.D. (登録日: 2007-01-23, 公開日: 2007-06-05, 最終更新日: 2023-08-30)

主引用文献

Wollert, T.,Pasche, B.,Rochon, M.,Deppenmeier, S.,van den Heuvel, J.,Gruber, A.D.,Heinz, D.W.,Lengeling, A.,Schubert, W.D.
Extending the host range of Listeria monocytogenes by rational protein design.
Cell(Cambridge,Mass.), 129:891-902, 2007

PubMed Abstract: In causing disease, pathogens outmaneuver host defenses through a dedicated arsenal of virulence determinants that specifically bind or modify individual host molecules. This dedication limits the intruder to a defined range of hosts. Newly emerging diseases mostly involve existing pathogens whose arsenal has been altered to allow them to infect previously inaccessible hosts. We have emulated this chance occurrence by extending the host range accessible to the human pathogen Listeria monocytogenes by the intestinal route to include the mouse. Analyzing the recognition complex of the listerial invasion protein InlA and its human receptor E-cadherin, we postulated and verified amino acid substitutions in InlA to increase its affinity for E-cadherin. Two single substitutions increase binding affinity by four orders of magnitude and extend binding specificity to include formerly incompatible murine E-cadherin. By rationally adapting a single protein, we thus create a versatile murine model of human listeriosis.

PubMed: 17540170
DOI: 10.1016/j.cell.2007.03.049

実験手法

X-RAY DIFFRACTION (1.9 Å)