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Reference Report
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| Citation | Mellroth, P., Karlsson, J., Hakansson, J., Schultz, N., Goldman, W.E., Steiner, H. (2005). Ligand-induced dimerization of Drosophila peptidoglycan recognition proteins in vitro. Proc. Natl. Acad. Sci. U.S.A. 102(18): 6455--6460. (Export to RIS) | ||
| FlyBase ID | FBrf0188267 | ||
| Publication Type | Research paper | ||
| PubMed ID | 15843462 | ||
| PubMed Abstract | Drosophila knockout mutants have placed peptidoglycan recognition proteins (PGRPs) in the two major pathways controlling immune gene expression. We now examine PGRP affinities for peptidoglycan. PGRP-SA and PGRP-LCx are bona fide pattern recognition receptors, and PGRP-SA, the peptidoglycan receptor of the Toll/Dif pathway, has selective affinity for different peptidoglycans. PGRP-LCx, the default peptidoglycan receptor of the Imd/Relish pathway, has strong affinity for all polymeric peptidoglycans tested and for monomeric peptidoglycan. PGRP-LCa does not have affinity for polymeric or monomeric peptidoglycan. Instead, PGRP-LCa can form heterodimers with LCx when the latter is bound to monomeric peptidoglycan. Hence, PGRP-LCa can be said to function as an adaptor, thus adding a new function to a member of the PGRP family. | ||
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| Language of Publication | English | ||
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| Publication Type | Journal | ||
| Abbreviation | Proc. Natl. Acad. Sci. U.S.A. | ||
| Title | Proceedings of the National Academy of Sciences of the United States of America | ||
| Publication Year | 1915- | ||
| ISBN/ISSN | 0027-8424 | ||
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Data from Reference
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| Alleles (3)
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| Genes (7)
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