3o4k

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[[Image:3o4k.png|left|200px]]
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==Crystal structure of the complex of peptidoglycan recognition protein (PGRP-S) and lipoteichoic acid at 2.1 A resolution==
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<StructureSection load='3o4k' size='340' side='right' caption='[[3o4k]], [[Resolution|resolution]] 2.11&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3o4k]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Camelus_dromedarius Camelus dromedarius]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O4K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3O4K FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=LTC:(2S)-1-({3-O-[2-(ACETYLAMINO)-4-AMINO-2,4,6-TRIDEOXY-BETA-D-GALACTOPYRANOSYL]-ALPHA-D-GLUCOPYRANOSYL}OXY)-3-(HEPTANOYLOXY)PROPAN-2-YL+(7Z)-PENTADEC-7-ENOATE'>LTC</scene>, <scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene><br>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3o4k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o4k OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3o4k RCSB], [http://www.ebi.ac.uk/pdbsum/3o4k PDBsum]</span></td></tr>
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<table>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o4/3o4k_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Peptidoglycan recognition proteins (PGRPs) are involved in the recognition of pathogen-associated molecular patterns. The well known pathogen-associated molecular patterns include LPS from Gram-negative bacteria and lipoteichoic acid (LTA) from Gram-positive bacteria. In this work, the crystal structures of two complexes of the short form of camel PGRP (CPGRP-S) with LPS and LTA determined at 1.7- and 2.1-A resolutions, respectively, are reported. Both compounds were held firmly inside the complex formed with four CPGRP-S molecules designated A, B, C, and D. The binding cleft is located at the interface of molecules C and D, which is extendable to the interface of molecules A and C. The interface of molecules A and B is tightly packed, whereas that of molecules B and D forms a wide channel. The hydrophilic moieties of these compounds occupy a common region, whereas hydrophobic chains interact with distinct regions in the binding site. The binding studies showed that CPGRP-S binds to LPS and LTA with affinities of 1.6 x 10(-9) and 2.4 x 10(-8) m, respectively. The flow cytometric studies showed that both LPS- and LTA-induced expression of the proinflammatory cytokines TNF-alpha and IL-6 was inhibited by CPGRP-S. The results of animal studies using mouse models indicated that both LPS- and LTA-induced mortality rates decreased drastically when CPGRP-S was administered. The recognition of both LPS and LTA, their high binding affinities for CPGRP-S, the significant decrease in the production of LPS- and LTA-induced TNF-alpha and IL-6, and the drastic reduction in the mortality rates in mice by CPGRP-S indicate its useful properties as an antibiotic agent.
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Structural Basis of Recognition of Pathogen-associated Molecular Patterns and Inhibition of Proinflammatory Cytokines by Camel Peptidoglycan Recognition Protein.,Sharma P, Dube D, Singh A, Mishra B, Singh N, Sinha M, Dey S, Kaur P, Mitra DK, Sharma S, Singh TP J Biol Chem. 2011 May 6;286(18):16208-17. Epub 2011 Mar 21. PMID:21454594<ref>PMID:21454594</ref>
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The line below this paragraph, containing "STRUCTURE_3o4k", creates the "Structure Box" on the page.
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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or leave the SCENE parameter empty for the default display.
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-->
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{{STRUCTURE_3o4k| PDB=3o4k | SCENE= }}
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===Crystal structure of the complex of peptidoglycan recognition protein (PGRP-S) and lipoteichoic acid at 2.1 A resolution===
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
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<!--
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<references/>
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The line below this paragraph, {{ABSTRACT_PUBMED_21454594}}, adds the Publication Abstract to the page
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__TOC__
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(as it appears on PubMed at http://www.pubmed.gov), where 21454594 is the PubMed ID number.
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</StructureSection>
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-->
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{{ABSTRACT_PUBMED_21454594}}
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==About this Structure==
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[[3o4k]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Camelus_dromedarius Camelus dromedarius]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O4K OCA].
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==Reference==
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<ref group="xtra">PMID:021454594</ref><references group="xtra"/>
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[[Category: Camelus dromedarius]]
[[Category: Camelus dromedarius]]
[[Category: Dube, D.]]
[[Category: Dube, D.]]

Revision as of 10:39, 28 May 2014

Crystal structure of the complex of peptidoglycan recognition protein (PGRP-S) and lipoteichoic acid at 2.1 A resolution

3o4k, resolution 2.11Å

Drag the structure with the mouse to rotate

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OCA

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