View source for 2rqe


==Solution structure of the silkworm bGRP/GNBP3 N-terminal domain reveals the mechanism for b-1,3-glucan specific recognition==
<StructureSection load='2rqe' size='340' side='right'caption='[[2rqe]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2rqe]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bombyx_mori Bombyx mori]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RQE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RQE FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2rqe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rqe OCA], [https://pdbe.org/2rqe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rqe RCSB], [https://www.ebi.ac.uk/pdbsum/2rqe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rqe ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/BGBP_BOMMO BGBP_BOMMO] Involved in the recognition of invading micro-organisms. Binds specifically to beta-1,3-glucan and activates the phenoloxidase cascade.<ref>PMID:10671539</ref> <ref>PMID:3136171</ref> 
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rq/2rqe_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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/main_output.php?pdb_ID=2rqe ConSurf].
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== Publication Abstract from PubMed ==
The beta-1,3-glucan recognition protein (betaGRP)/Gram-negative bacteria-binding protein 3 (GNBP3) is a crucial pattern-recognition receptor that specifically binds beta-1,3-glucan, a component of fungal cell walls. It evokes innate immunity against fungi through activation of the prophenoloxidase (proPO) cascade and Toll pathway in invertebrates. The betaGRP consists of an N-terminal beta-1,3-glucan-recognition domain and a C-terminal glucanase-like domain, with the former reported to be responsible for the proPO cascade activation. This report shows the solution structure of the N-terminal beta-1,3-glucan recognition domain of silkworm betaGRP. Although the N-terminal domain of betaGRP has a beta-sandwich fold, often seen in carbohydrate-binding modules, both NMR titration experiments and mutational analysis showed that betaGRP has a binding mechanism which is distinct from those observed in previously reported carbohydarate-binding domains. Our results suggest that betaGRP is a beta-1,3-glucan-recognition protein that specifically recognizes a triple-helical structure of beta-1,3-glucan.

Solution structure of the silkworm betaGRP/GNBP3 N-terminal domain reveals the mechanism for beta-1,3-glucan-specific recognition.,Takahasi K, Ochiai M, Horiuchi M, Kumeta H, Ogura K, Ashida M, Inagaki F Proc Natl Acad Sci U S A. 2009 Jul 14;106(28):11679-84. Epub 2009 Jun 26. PMID:19561300<ref>PMID:19561300</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 2rqe" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bombyx mori]]
[[Category: Large Structures]]
[[Category: Ashida M]]
[[Category: Horiuchi M]]
[[Category: Inagaki F]]
[[Category: Kumeta H]]
[[Category: Ochiai M]]
[[Category: Ogura K]]
[[Category: Takahasi K]]