2rqe: Difference between revisions

Latest revision as of 19:15, 29 May 2024

Solution structure of the silkworm bGRP/GNBP3 N-terminal domain reveals the mechanism for b-1,3-glucan specific recognition

Structural highlights

2rqe is a 1 chain structure with sequence from Bombyx mori. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

BGBP_BOMMO Involved in the recognition of invading micro-organisms. Binds specifically to beta-1,3-glucan and activates the phenoloxidase cascade.^[1] ^[2]

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

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^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Ochiai M, Ashida M. A pattern-recognition protein for beta-1,3-glucan. The binding domain and the cDNA cloning of beta-1,3-glucan recognition protein from the silkworm, Bombyx mori. J Biol Chem. 2000 Feb 18;275(7):4995-5002. PMID:10671539
↑ Ochiai M, Ashida M. Purification of a beta-1,3-glucan recognition protein in the prophenoloxidase activating system from hemolymph of the silkworm, Bombyx mori. J Biol Chem. 1988 Aug 25;263(24):12056-62. PMID:3136171
↑ Takahasi K, Ochiai M, Horiuchi M, Kumeta H, Ogura K, Ashida M, Inagaki F. Solution structure of the silkworm betaGRP/GNBP3 N-terminal domain reveals the mechanism for beta-1,3-glucan-specific recognition. Proc Natl Acad Sci U S A. 2009 Jul 14;106(28):11679-84. Epub 2009 Jun 26. PMID:19561300

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OCA

[1] Ochiai M, Ashida M. A pattern-recognition protein for beta-1,3-glucan. The binding domain and the cDNA cloning of beta-1,3-glucan recognition protein from the silkworm, Bombyx mori. J Biol Chem. 2000 Feb 18;275(7):4995-5002. PMID:10671539

[2] Ochiai M, Ashida M. Purification of a beta-1,3-glucan recognition protein in the prophenoloxidase activating system from hemolymph of the silkworm, Bombyx mori. J Biol Chem. 1988 Aug 25;263(24):12056-62. PMID:3136171

[3] Takahasi K, Ochiai M, Horiuchi M, Kumeta H, Ogura K, Ashida M, Inagaki F. Solution structure of the silkworm betaGRP/GNBP3 N-terminal domain reveals the mechanism for beta-1,3-glucan-specific recognition. Proc Natl Acad Sci U S A. 2009 Jul 14;106(28):11679-84. Epub 2009 Jun 26. PMID:19561300

[1]

[2]

[3]

@@ Line 1: / Line 1: @@
 ==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]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<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 [http://en.wikipedia.org/wiki/Bommo Bommo]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2RQE FirstGlance]. <br>
+<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='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=2rqe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rqe OCA], [http://pdbe.org/2rqe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2rqe RCSB], [http://www.ebi.ac.uk/pdbsum/2rqe PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2rqe ProSAT]</span></td></tr>
+</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 ==
-[[http://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>
+[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]]
@@ Line 31: / Line 32: @@
 __TOC__
 </StructureSection>
-[[Category: Bommo]]
+[[Category: Bombyx mori]]
-[[Category: Ashida, M]]
+[[Category: Large Structures]]
-[[Category: Horiuchi, M]]
+[[Category: Ashida M]]
-[[Category: Inagaki, F]]
+[[Category: Horiuchi M]]
-[[Category: Kumeta, H]]
+[[Category: Inagaki F]]
-[[Category: Ochiai, M]]
+[[Category: Kumeta H]]
-[[Category: Ogura, K]]
+[[Category: Ochiai M]]
-[[Category: Takahasi, K]]
+[[Category: Ogura K]]
-[[Category: 3-glucan]]
+[[Category: Takahasi K]]
-[[Category: Beta-1]]
-[[Category: Glycoprotein]]
-[[Category: Immune response]]
-[[Category: Innate immunity]]
-[[Category: Protein]]
-[[Category: Secreted]]
-[[Category: Sugar binding protein]]

2rqe: Difference between revisions

Latest revision as of 19:15, 29 May 2024

Solution structure of the silkworm bGRP/GNBP3 N-terminal domain reveals the mechanism for b-1,3-glucan specific recognition

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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