Abstract
The family of peptidoglycan recognition proteins (PGRPs) are associated with the recognition of the peptidoglycan of microbes and subsequent activation of signaling pathways for immune response. Here the crystal structure of Drosophila PGRP-LB is determined at a resolution of 2.0 Å and shows an active-site cleft with a zinc cage. Poor conservation of surface residues at the cleft predicts a widely varying individual specificity of PGRPs for molecular patterns on microbial cell walls. At the back of this cleft is a putatively conserved distinctive groove. The location and mainly hydrophobic nature of the groove indicate that the back face serves for subsequent signaling after clustering of PGRP molecules by binding to polymeric cell wall components.
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Acknowledgements
We thank H. Robinson for the Mail-in x-ray data collection and preliminary processing at the Brookhaven National Laboratory, Biology beamline X25, at the National Synchrotron Light Source. This study was supported by Creative Research Initiatives of the Korean Ministry of Science & Technology. M.-S.K. was supported by the Brain Korea 21 Project. The Brookhaven National Laboratory Biology PX Mail-in program is supported by the National Institutes of Health, National Center for Research Resources.
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Kim, MS., Byun, M. & Oh, BH. Crystal structure of peptidoglycan recognition protein LB from Drosophila melanogaster. Nat Immunol 4, 787–793 (2003). https://doi.org/10.1038/ni952
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DOI: https://doi.org/10.1038/ni952
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