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2d7f

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Revision as of 04:00, 10 September 2015

Crystal structure of A lectin from canavalia gladiata seeds complexed with alpha-methyl-mannoside and alpha-aminobutyric acid

Structural highlights

2d7f is a 4 chain structure with sequence from Canavalia gladiata. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , ,
Related:	1wuv
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[CONA_CANGL] Glucose/D-mannose/rhamnose specific lectin. Has hemagglutinating activity towards rabbit erythrocytes. Has mitogenic activity towards murine splenocytes that is inhibited by glucose. Inhibits HIV-1 reverse transcriptase with an IC(50) of 35uM. Has a potent antiproliferative activity against L1210 leukemia cells in vitro that is not inhibited by glucose. Inhibits translation in cell-free rabbit reticulocyte system with an IC(50) of 2.08uM. Lacks anti-fungal activity against M.arachidicola, B.cenera and F.oxysporum.^[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

BACKGROUND: Lectins are mainly described as simple carbohydrate-binding proteins. Previous studies have tried to identify other binding sites, which possible recognize plant hormones, secondary metabolites, and isolated amino acid residues. We report the crystal structure of a lectin isolated from Canavalia gladiata seeds (CGL), describing a new binding pocket, which may be related to pathogen resistance activity in ConA-like lectins; a site where a non-protein amino-acid, alpha-aminobutyric acid (Abu), is bound. RESULTS: The overall structure of native CGL and complexed with alpha-methyl-mannoside and Abu have been refined at 2.3 A and 2.31 A resolution, respectively. Analysis of the electron density maps of the CGL structure shows clearly the presence of Abu, which was confirmed by mass spectrometry. CONCLUSION: The presence of Abu in a plant lectin structure strongly indicates the ability of lectins on carrying secondary metabolites. Comparison of the amino acids composing the site with other legume lectins revealed that this site is conserved, providing an evidence of the biological relevance of this site. This new action of lectins strengthens their role in defense mechanisms in plants.

Structure of a lectin from Canavalia gladiata seeds: new structural insights for old molecules.,Delatorre P, Rocha BA, Souza EP, Oliveira TM, Bezerra GA, Moreno FB, Freitas BT, Santi-Gadelha T, Sampaio AH, Azevedo WF Jr, Cavada BS BMC Struct Biol. 2007 Aug 2;7:52. PMID:17683532^[2]

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

References

↑ Wong JH, Ng TB. Isolation and characterization of a glucose/mannose/rhamnose-specific lectin from the knife bean Canavalia gladiata. Arch Biochem Biophys. 2005 Jul 1;439(1):91-8. PMID:15935326 doi:http://dx.doi.org/S0003-9861(05)00186-4
↑ Delatorre P, Rocha BA, Souza EP, Oliveira TM, Bezerra GA, Moreno FB, Freitas BT, Santi-Gadelha T, Sampaio AH, Azevedo WF Jr, Cavada BS. Structure of a lectin from Canavalia gladiata seeds: new structural insights for old molecules. BMC Struct Biol. 2007 Aug 2;7:52. PMID:17683532 doi:10.1186/1472-6807-7-52

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2d7f"

@@ Line 5: / Line 5: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=DBB:D-ALPHA-AMINOBUTYRIC+ACID'>DBB</scene>, <scene name='pdbligand=MMA:O1-METHYL-MANNOSE'>MMA</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1wuv|1wuv]]</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=2d7f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d7f OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2d7f RCSB], [http://www.ebi.ac.uk/pdbsum/2d7f 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=2d7f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d7f OCA], [http://pdbe.org/2d7f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2d7f RCSB], [http://www.ebi.ac.uk/pdbsum/2d7f PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 27: / Line 27: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2d7f" style="background-color:#fffaf0;"></div>
 ==See Also==

2d7f

From Proteopedia

Revision as of 04:00, 10 September 2015

Crystal structure of A lectin from canavalia gladiata seeds complexed with alpha-methyl-mannoside and alpha-aminobutyric acid

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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