Structure of tracheal cytotoxin in complex with a heterodimeric pattern-recognition receptor

Chung I. Chang, Yogarany Chelliah, Dominika Borek, Dominique Mengin-Lecreulx, Johann Deisanhofer

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Abstract

Tracheal cytotoxin (TCT), a naturally occurring fragment of Gram-negative peptidoglycan, is a potent elicitor of innate immune responses in Drosophila. It induces the heterodimerization of its recognition receptors, the peptidoglycan recognition proteins (PGRPs) LCa and LCx, which activates the immune deficiency pathway. The crystal structure at 2.1 angstrom resolution of TCT in complex with the ectodomains of PGRP-LCa and PGRP-LCx shows that TCT is bound to and presented by the LCx ectodomain for recognition by the LCa ectodomain; the latter lacks a canonical peptidoglycan-docking groove conserved in other PGRPs. The interface, revealed in atomic detail, between TCT and the receptor complex highlights the importance of the anhydro-containing disaccharide in bridging the two ectodomains together and the critical role of diaminopimelic acid as the specificity determinant for PGRP interaction.

Original languageEnglish (US)
Pages (from-to)1761-1764
Number of pages4
JournalScience
Volume311
Issue number5768
DOIs
StatePublished - Mar 24 2006

ASJC Scopus subject areas

  • General

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    Chang, C. I., Chelliah, Y., Borek, D., Mengin-Lecreulx, D., & Deisanhofer, J. (2006). Structure of tracheal cytotoxin in complex with a heterodimeric pattern-recognition receptor. Science, 311(5768), 1761-1764. https://doi.org/10.1126/science.1123056