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[[Image:2ef6.gif|left|200px]]


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==Canavalia gladiata lectin complexed with Man1-3Man-OMe==
The line below this paragraph, containing "STRUCTURE_2ef6", creates the "Structure Box" on the page.
<StructureSection load='2ef6' size='340' side='right'caption='[[2ef6]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[2ef6]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Canavalia_gladiata Canavalia gladiata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EF6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2EF6 FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
-->
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=MMA:O1-METHYL-MANNOSE'>MMA</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
{{STRUCTURE_2ef6|  PDB=2ef6  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ef6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ef6 OCA], [https://pdbe.org/2ef6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ef6 RCSB], [https://www.ebi.ac.uk/pdbsum/2ef6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ef6 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CONA_CANGL 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.<ref>PMID:15935326</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/ef/2ef6_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=2ef6 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Plant lectins, especially those purified from species of the Leguminosae family, represent the best studied group of carbohydrate-binding proteins. The legume lectins from Diocleinae subtribe are highly similar proteins that present significant differences in the potency/efficacy of their biological activities. The structural studies of the interactions between lectins and sugars may clarify the origin of the distinct biological activities observed in this high similar class of proteins. In this way, this work presents a crystallographic study of the ConM and CGL (agglutinins from Canavalia maritima and Canavalia gladiata, respectively) in the following complexes: ConM/CGL:Man(alpha1-2)Man(alpha1-O)Me, ConM/CGL:Man(alpha1-3)Man(alpha1-O)Me and ConM/CGL:Man(alpha1-4)Man(alpha1-O)Me, which crystallized in different conditions and space group from the native proteins. The structures were solved by molecular replacement, presenting satisfactory values for R(factor) and R(free). Comparisons between ConM, CGL and ConA (Canavalia ensiformis lectin) binding mode with the dimannosides in subject, presented different interactions patterns, which may account for a structural explanation of the distincts biological properties observed in the lectins of Diocleinae subtribe.


'''Canavalia gladiata lectin complexed with Man1-3Man-OMe'''
Structural analysis of Canavalia maritima and Canavalia gladiata lectins complexed with different dimannosides: new insights into the understanding of the structure-biological activity relationship in legume lectins.,Bezerra GA, Oliveira TM, Moreno FB, de Souza EP, da Rocha BA, Benevides RG, Delatorre P, de Azevedo WF Jr, Cavada BS J Struct Biol. 2007 Nov;160(2):168-76. Epub 2007 Aug 16. PMID:17881248<ref>PMID:17881248</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2ef6" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
Plant lectins, especially those purified from species of the Leguminosae family, represent the best studied group of carbohydrate-binding proteins. The legume lectins from Diocleinae subtribe are highly similar proteins that present significant differences in the potency/efficacy of their biological activities. The structural studies of the interactions between lectins and sugars may clarify the origin of the distinct biological activities observed in this high similar class of proteins. In this way, this work presents a crystallographic study of the ConM and CGL (agglutinins from Canavalia maritima and Canavalia gladiata, respectively) in the following complexes: ConM/CGL:Man(alpha1-2)Man(alpha1-O)Me, ConM/CGL:Man(alpha1-3)Man(alpha1-O)Me and ConM/CGL:Man(alpha1-4)Man(alpha1-O)Me, which crystallized in different conditions and space group from the native proteins. The structures were solved by molecular replacement, presenting satisfactory values for R(factor) and R(free). Comparisons between ConM, CGL and ConA (Canavalia ensiformis lectin) binding mode with the dimannosides in subject, presented different interactions patterns, which may account for a structural explanation of the distincts biological properties observed in the lectins of Diocleinae subtribe.
*[[Concanavalin 3D structures|Concanavalin 3D structures]]
 
== References ==
==About this Structure==
<references/>
2EF6 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Canavalia_gladiata Canavalia gladiata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EF6 OCA].
__TOC__
 
</StructureSection>
==Reference==
Structural analysis of Canavalia maritima and Canavalia gladiata lectins complexed with different dimannosides: new insights into the understanding of the structure-biological activity relationship in legume lectins., Bezerra GA, Oliveira TM, Moreno FB, de Souza EP, da Rocha BA, Benevides RG, Delatorre P, de Azevedo WF Jr, Cavada BS, J Struct Biol. 2007 Nov;160(2):168-76. Epub 2007 Aug 16. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17881248 17881248]
[[Category: Canavalia gladiata]]
[[Category: Single protein]]
[[Category: Benevides, R G.]]
[[Category: Bezerra, G A.]]
[[Category: Cavada, B S.]]
[[Category: Delatorre, P.]]
[[Category: Jr., W F.de Azevedo.]]
[[Category: Moreno, F B.M B.]]
[[Category: Oliveira, T M.]]
[[Category: Rocha, B A.M da.]]
[[Category: Souza, E P.de.]]
[[Category: Canavalia gladiata]]
[[Category: Canavalia gladiata]]
[[Category: Dimannoside]]
[[Category: Large Structures]]
[[Category: Lectin]]
[[Category: Benevides RG]]
[[Category: Plant protein]]
[[Category: Bezerra GA]]
[[Category: Seed]]
[[Category: Cavada BS]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 02:27:25 2008''
[[Category: Delatorre P]]
[[Category: Moreno FBMB]]
[[Category: Oliveira TM]]
[[Category: Da Rocha BAM]]
[[Category: De Azevedo Jr WF]]
[[Category: De Souza EP]]

Latest revision as of 11:39, 25 October 2023

Canavalia gladiata lectin complexed with Man1-3Man-OMeCanavalia gladiata lectin complexed with Man1-3Man-OMe

Structural highlights

2ef6 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.
Method:X-ray diffraction, Resolution 2.1Å
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

Plant lectins, especially those purified from species of the Leguminosae family, represent the best studied group of carbohydrate-binding proteins. The legume lectins from Diocleinae subtribe are highly similar proteins that present significant differences in the potency/efficacy of their biological activities. The structural studies of the interactions between lectins and sugars may clarify the origin of the distinct biological activities observed in this high similar class of proteins. In this way, this work presents a crystallographic study of the ConM and CGL (agglutinins from Canavalia maritima and Canavalia gladiata, respectively) in the following complexes: ConM/CGL:Man(alpha1-2)Man(alpha1-O)Me, ConM/CGL:Man(alpha1-3)Man(alpha1-O)Me and ConM/CGL:Man(alpha1-4)Man(alpha1-O)Me, which crystallized in different conditions and space group from the native proteins. The structures were solved by molecular replacement, presenting satisfactory values for R(factor) and R(free). Comparisons between ConM, CGL and ConA (Canavalia ensiformis lectin) binding mode with the dimannosides in subject, presented different interactions patterns, which may account for a structural explanation of the distincts biological properties observed in the lectins of Diocleinae subtribe.

Structural analysis of Canavalia maritima and Canavalia gladiata lectins complexed with different dimannosides: new insights into the understanding of the structure-biological activity relationship in legume lectins.,Bezerra GA, Oliveira TM, Moreno FB, de Souza EP, da Rocha BA, Benevides RG, Delatorre P, de Azevedo WF Jr, Cavada BS J Struct Biol. 2007 Nov;160(2):168-76. Epub 2007 Aug 16. PMID:17881248[2]

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

See Also

References

  1. ↑ 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
  2. ↑ Bezerra GA, Oliveira TM, Moreno FB, de Souza EP, da Rocha BA, Benevides RG, Delatorre P, de Azevedo WF Jr, Cavada BS. Structural analysis of Canavalia maritima and Canavalia gladiata lectins complexed with different dimannosides: new insights into the understanding of the structure-biological activity relationship in legume lectins. J Struct Biol. 2007 Nov;160(2):168-76. Epub 2007 Aug 16. PMID:17881248 doi:http://dx.doi.org/10.1016/j.jsb.2007.07.012

2ef6, resolution 2.10Å

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