1twq

<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>

</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>

<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='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='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>

[[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>

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== 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<ref>PMID:15572450</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1twq" style="background-color:#fffaf0;"></div>

[[Category: Human]]

[[Category: Boons, G A]]

[[Category: Guan, R]]

[[Category: Mariuzza, R A]]

[[Category: Roychowdury, A]]

[[Category: Pgrp-ialpha]]