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| | <StructureSection load='1twq' size='340' side='right'caption='[[1twq]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='1twq' size='340' side='right'caption='[[1twq]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1twq]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TWQ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1TWQ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1twq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TWQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TWQ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=AMU:BETA-N-ACETYLMURAMIC+ACID'>AMU</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=GMA:4-AMIDO-4-CARBAMOYL-BUTYRIC+ACID'>GMA</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AMU:BETA-N-ACETYLMURAMIC+ACID'>AMU</scene>, <scene name='pdbligand=GMA:4-AMIDO-4-CARBAMOYL-BUTYRIC+ACID'>GMA</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1sk3|1sk3]], [[1sk4|1sk4]]</div></td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1twq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1twq OCA], [https://pdbe.org/1twq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1twq RCSB], [https://www.ebi.ac.uk/pdbsum/1twq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1twq ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PGLYRP3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1twq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1twq OCA], [http://pdbe.org/1twq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1twq RCSB], [http://www.ebi.ac.uk/pdbsum/1twq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1twq ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PGRP3_HUMAN PGRP3_HUMAN]] Pattern receptor that binds to murein peptidoglycans (PGN) of Gram-positive bacteria. Has bactericidal activity towards Gram-positive bacteria. May kill Gram-positive bacteria by interfering with peptidoglycan biosynthesis. Binds also to Gram-negative bacteria, and has bacteriostatic activity towards Gram-negative bacteria. Plays a role in innate immunity.<ref>PMID:16354652</ref> | + | [https://www.uniprot.org/uniprot/PGRP3_HUMAN PGRP3_HUMAN] Pattern receptor that binds to murein peptidoglycans (PGN) of Gram-positive bacteria. Has bactericidal activity towards Gram-positive bacteria. May kill Gram-positive bacteria by interfering with peptidoglycan biosynthesis. Binds also to Gram-negative bacteria, and has bacteriostatic activity towards Gram-negative bacteria. Plays a role in innate immunity.<ref>PMID:16354652</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Boons, G A]] | + | [[Category: Boons G-A]] |
| - | [[Category: Guan, R]] | + | [[Category: Guan R]] |
| - | [[Category: Mariuzza, R A]] | + | [[Category: Mariuzza RA]] |
| - | [[Category: Roychowdury, A]] | + | [[Category: Roychowdury A]] |
| - | [[Category: Complex]]
| + | |
| - | [[Category: Crystal structure]]
| + | |
| - | [[Category: Immune system]]
| + | |
| - | [[Category: Membrane protein]]
| + | |
| - | [[Category: Pgn analog]]
| + | |
| - | [[Category: Pgrp]]
| + | |
| - | [[Category: Pgrp-ialpha]]
| + | |
| Structural highlights
Function
PGRP3_HUMAN Pattern receptor that binds to murein peptidoglycans (PGN) of Gram-positive bacteria. Has bactericidal activity towards Gram-positive bacteria. May kill Gram-positive bacteria by interfering with peptidoglycan biosynthesis. Binds also to Gram-negative bacteria, and has bacteriostatic activity towards Gram-negative bacteria. Plays a role in innate immunity.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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-A resolution, of the C-terminal PGN-binding domain of human PGRP-Ialpha 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-acetylmuramic acid situated in the middle of the groove, whose shallow end can accommodate a linked 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(2+)-containing PGRPs.
Structural basis for peptidoglycan binding by peptidoglycan recognition proteins.,Guan R, Roychowdhury A, Ember B, Kumar S, Boons GJ, Mariuzza RA Proc Natl Acad Sci U S A. 2004 Dec 7;101(49):17168-73. Epub 2004 Nov 30. PMID:15572450[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lu X, Wang M, Qi J, Wang H, Li X, Gupta D, Dziarski R. Peptidoglycan recognition proteins are a new class of human bactericidal proteins. J Biol Chem. 2006 Mar 3;281(9):5895-907. Epub 2005 Dec 14. PMID:16354652 doi:http://dx.doi.org/10.1074/jbc.M511631200
- ↑ Guan R, Roychowdhury A, Ember B, Kumar S, Boons GJ, Mariuzza RA. Structural basis for peptidoglycan binding by peptidoglycan recognition proteins. Proc Natl Acad Sci U S A. 2004 Dec 7;101(49):17168-73. Epub 2004 Nov 30. PMID:15572450
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