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Protein Science (2006), 15:1199-1206. Published by Cold Spring Harbor Laboratory Press. Copyright © 2006 The Protein Society
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FOR THE RECORD

Crystal structure of human peptidoglycan recognition protein I{alpha} bound to a muramyl pentapeptide from Gram-positive bacteria

Rongjin Guan1, Patrick H. Brown1, Chittoor P. Swaminathan1, Abhijit Roychowdhury2, Geert-Jan Boons2 and Roy A. Mariuzza1

1 Center for Advanced Research in Biotechnology, W.M. Keck Laboratory for Structural Biology, University of Maryland Biotechnology Institute, Rockville, Maryland 20850, USA
2 Complex Carbohydrate Research Center, University of Georgia, Athens, Georgia 30602, USA

(RECEIVED January 5, 2006; FINAL REVISION February 16, 2006; ACCEPTED February 16, 2006)

Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors of the innate immune system that bind bacterial peptidoglycans (PGNs). We determined the crystal structure, to 2.1 Å resolution, of the C-terminal PGN-binding domain of human PGRP-I{alpha} in complex with a muramyl pentapeptide (MPP) from Gram-positive bacteria containing a complete peptide stem (L-Ala-D-isoGln-L-Lys-D-Ala-D-Ala). The structure reveals important features not observed previously in the complex between PGRP-I{alpha} and a muramyl tripeptide lacking D-Ala at stem positions 4 and 5. Most notable are ligand-induced structural rearrangements in the PGN-binding site that are essential for entry of the C-terminal portion of the peptide stem and for locking MPP in the binding groove. We propose that similar structural rearrangements to accommodate the PGN stem likely characterize many PGRPs, both mammalian and insect.

Keywords: bacteria; crystal structure; innate immunity; peptidoglycan; PGRP


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