1YCK

Crystal structure of human peptidoglycan recognition protein (PGRP-S)

Summary for 1YCK

• Entry DOI: 10.2210/pdb1yck/pdb
• Related: 1OHT 1S2J 1SK3 1SK4 1SXR 1TWQ
• Descriptor: Peptidoglycan recognition protein (2 entities in total)
• Functional Keywords: pgrp-s, peptidoglycan recognition, innate immunity, pattern recognition proteins, immune system
• Biological source: Homo sapiens (human)
• Cellular location: Secreted: O75594
• Total number of polymer chains: 1
• Total formula weight: 19456.94

Authors

Guan, R.,Wang, Q.,Sundberg, E.J.,Mariuzza, R.A. (deposition date: 2004-12-22, release date: 2005-03-22, Last modification date: 2024-10-30)

Primary citation

Guan, R.,Wang, Q.,Sundberg, E.J.,Mariuzza, R.A.
Crystal structure of human peptidoglycan recognition protein S (PGRP-S) at 1.70 A resolution.
J.Mol.Biol., 347:683-691, 2005

PubMed Abstract: Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors of the innate immune system that bind peptidoglycans (PGNs) of bacterial cell walls. These molecules, which are highly conserved from insects to mammals, contribute to host defense against infections by both Gram-positive and Gram-negative bacteria. Here, we present the crystal structure of human PGRP-S at 1.70A resolution. The overall structure of PGRP-S, which participates in intracellular killing of Gram-positive bacteria, is similar to that of other PGRPs, including Drosophila PGRP-LB and PGRP-SA and human PGRP-Ialpha. However, comparison with these PGRPs reveals important differences in both the PGN-binding site and a groove formed by the PGRP-specific segment on the opposite face of the molecule. This groove, which may constitute a binding site for effector or signaling proteins, is less hydrophobic and deeper in PGRP-S than in PGRP-IalphaC, whose PGRP-specific segments vary considerably in amino acid sequence. By docking a PGN ligand into the PGN-binding cleft of PGRP-S based on the known structure of a PGRP-Ialpha-PGN complex, we identified potential PGN-binding residues in PGRP-S. Differences in PGN-contacting residues and interactions suggest that, although PGRPs may engage PGNs in a similar mode, structural differences exist that likely regulate the affinity and fine specificity of PGN recognition.

PubMed: 15769462
DOI: 10.1016/j.jmb.2005.01.070

Experimental method

X-RAY DIFFRACTION (1.7 Å)