1yck
From Proteopedia
(New page: 200px<br /> <applet load="1yck" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yck, resolution 1.70Å" /> '''Crystal structure o...) |
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| - | [[Image:1yck.gif|left|200px]]<br /> | + | [[Image:1yck.gif|left|200px]]<br /><applet load="1yck" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1yck" size=" | + | |
caption="1yck, resolution 1.70Å" /> | caption="1yck, resolution 1.70Å" /> | ||
'''Crystal structure of human peptidoglycan recognition protein (PGRP-S)'''<br /> | '''Crystal structure of human peptidoglycan recognition protein (PGRP-S)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Peptidoglycan recognition proteins (PGRPs) are pattern recognition | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1YCK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1YCK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YCK OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Guan, R.]] | [[Category: Guan, R.]] | ||
| - | [[Category: Mariuzza, R | + | [[Category: Mariuzza, R A.]] |
| - | [[Category: Sundberg, E | + | [[Category: Sundberg, E J.]] |
[[Category: Wang, Q.]] | [[Category: Wang, Q.]] | ||
[[Category: crystal structure]] | [[Category: crystal structure]] | ||
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[[Category: pgrp-s]] | [[Category: pgrp-s]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:03:58 2008'' |
Revision as of 14:03, 21 February 2008
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Crystal structure of human peptidoglycan recognition protein (PGRP-S)
Overview
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.
About this Structure
1YCK is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of human peptidoglycan recognition protein S (PGRP-S) at 1.70 A resolution., Guan R, Wang Q, Sundberg EJ, Mariuzza RA, J Mol Biol. 2005 Apr 8;347(4):683-91. PMID:15769462
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