{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,15]],"date-time":"2026-04-15T07:16:21Z","timestamp":1776237381158,"version":"3.50.1"},"reference-count":41,"publisher":"Proceedings of the National Academy of Sciences","issue":"49","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2004,12,7]]},"abstract":"<jats:p>\n            Peptidoglycan (PGN) recognition proteins (PGRPs) are pattern-recognition receptors of the innate immune system that bind and, in some cases, hydrolyze bacterial PGNs. We determined the crystal structure, at 2.30-\u00c5 resolution, of the C-terminal PGN-binding domain of human PGRP-I\u03b1 in complex with a muramyl tripeptide representing the core of lysine-type PGNs from Gram-positive bacteria. The peptide stem of the ligand is buried at the deep end of a long binding groove, with\n            <jats:italic>N<\/jats:italic>\n            -acetylmuramic acid situated in the middle of the groove, whose shallow end can accommodate a linked\n            <jats:italic>N<\/jats:italic>\n            -acetylglucosamine. Although most interactions are with the peptide, the glycan moiety also seems to be essential for specific recognition by PGRPs. Conservation of key PGN-contacting residues shows that all PGRPs employ this basic PGN-binding mode. The structure pinpoints variable residues that likely mediate discrimination between lysine- and diaminopimelic acid-type PGNs. We also propose a mechanism for PGN hydrolysis by Zn\n            <jats:sup>2+<\/jats:sup>\n            -containing PGRPs.\n          <\/jats:p>","DOI":"10.1073\/pnas.0407856101","type":"journal-article","created":{"date-parts":[[2004,12,1]],"date-time":"2004-12-01T01:14:05Z","timestamp":1101863645000},"page":"17168-17173","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":114,"title":["Structural basis for peptidoglycan binding by peptidoglycan recognition proteins"],"prefix":"10.1073","volume":"101","author":[{"given":"Rongjin","family":"Guan","sequence":"first","affiliation":[{"name":"Center for Advanced Research in Biotechnology, W. M. Keck Laboratory for Structural Biology, University of Maryland Biotechnology Institute, Rockville, MD 20850; and Complex Carbohydrate Research Center, University of Georgia, 315 Riverbend Road, Athens, GA 30602"}]},{"given":"Abhijit","family":"Roychowdhury","sequence":"additional","affiliation":[{"name":"Center for Advanced Research in Biotechnology, W. M. Keck Laboratory for Structural Biology, University of Maryland Biotechnology Institute, Rockville, MD 20850; and Complex Carbohydrate Research Center, University of Georgia, 315 Riverbend Road, Athens, GA 30602"}]},{"given":"Brian","family":"Ember","sequence":"additional","affiliation":[{"name":"Center for Advanced Research in Biotechnology, W. M. Keck Laboratory for Structural Biology, University of Maryland Biotechnology Institute, Rockville, MD 20850; and Complex Carbohydrate Research Center, University of Georgia, 315 Riverbend Road, Athens, GA 30602"}]},{"given":"Sanjay","family":"Kumar","sequence":"additional","affiliation":[{"name":"Center for Advanced Research in Biotechnology, W. M. Keck Laboratory for Structural Biology, University of Maryland Biotechnology Institute, Rockville, MD 20850; and Complex Carbohydrate Research Center, University of Georgia, 315 Riverbend Road, Athens, GA 30602"}]},{"given":"Geert-Jan","family":"Boons","sequence":"additional","affiliation":[{"name":"Center for Advanced Research in Biotechnology, W. M. Keck Laboratory for Structural Biology, University of Maryland Biotechnology Institute, Rockville, MD 20850; and Complex Carbohydrate Research Center, University of Georgia, 315 Riverbend Road, Athens, GA 30602"}]},{"given":"Roy A.","family":"Mariuzza","sequence":"additional","affiliation":[{"name":"Center for Advanced Research in Biotechnology, W. M. Keck Laboratory for Structural Biology, University of Maryland Biotechnology Institute, Rockville, MD 20850; and Complex Carbohydrate Research Center, University of Georgia, 315 Riverbend Road, Athens, GA 30602"}]}],"member":"341","published-online":{"date-parts":[[2004,11,30]]},"reference":[{"key":"e_1_3_2_1_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.1068883"},{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1038\/nature02021"},{"key":"e_1_3_2_3_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1600-065X.1998.tb01185.x"},{"key":"e_1_3_2_4_2","doi-asserted-by":"publisher","DOI":"10.1093\/glycob\/11.3.25R"},{"key":"e_1_3_2_5_2","doi-asserted-by":"crossref","unstructured":"Doyle R. J. & Dziarski R. (2001) in Molecular Medical Microbiology ed. Sussman M. 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