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2aph

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Revision as of 06:24, 4 April 2018

Crystal structure of human PGRP-IalphaC in complex with muramyl pentapeptide

Structural highlights

2aph is a 4 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
NonStd Res:	, ,
Related:	1sk3, 1sk4
Gene:	PGLYRP3, PGRPIA (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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 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 A 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.

Crystal structure of human peptidoglycan recognition protein I alpha bound to a muramyl pentapeptide from Gram-positive bacteria.,Guan R, Brown PH, Swaminathan CP, Roychowdhury A, Boons GJ, Mariuzza RA Protein Sci. 2006 May;15(5):1199-206. PMID:16641493^[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, Brown PH, Swaminathan CP, Roychowdhury A, Boons GJ, Mariuzza RA. Crystal structure of human peptidoglycan recognition protein I alpha bound to a muramyl pentapeptide from Gram-positive bacteria. Protein Sci. 2006 May;15(5):1199-206. PMID:16641493 doi:15/5/1199

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2aph"

@@ Line 1: / Line 1: @@
 ==Crystal structure of human PGRP-IalphaC in complex with muramyl pentapeptide==
 <StructureSection load='2aph' size='340' side='right' caption='[[2aph]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
@@ Line 7: / Line 8: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1sk3|1sk3]], [[1sk4|1sk4]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PGLYRP3, PGRPIA ([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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2aph FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2aph OCA], [http://pdbe.org/2aph PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2aph RCSB], [http://www.ebi.ac.uk/pdbsum/2aph PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2aph FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2aph OCA], [http://pdbe.org/2aph PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2aph RCSB], [http://www.ebi.ac.uk/pdbsum/2aph PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2aph ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 15: / Line 16: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ap/2aph_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ap/2aph_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

2aph

From Proteopedia

Revision as of 06:24, 4 April 2018

Crystal structure of human PGRP-IalphaC in complex with muramyl pentapeptide

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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