2f2l

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2f2l, resolution 2.10Å

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Crystal structure of tracheal cytotoxin (TCT) bound to the ectodomain complex of peptidoglycan recognition proteins LCa (PGRP-LCa) and LCx (PGRP-LCx)

Overview

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.

About this Structure

2F2L is a Protein complex structure of sequences from Drosophila melanogaster with NAG, SO4, MLD and CIT as ligands. Full crystallographic information is available from OCA.

Reference

Structure of tracheal cytotoxin in complex with a heterodimeric pattern-recognition receptor., Chang CI, Chelliah Y, Borek D, Mengin-Lecreulx D, Deisenhofer J, Science. 2006 Mar 24;311(5768):1761-4. PMID:16556841

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