2zbj: Difference between revisions
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< | ==Crystal structure of Dioclea rostrata lectin== | ||
<StructureSection load='2zbj' size='340' side='right'caption='[[2zbj]], [[Resolution|resolution]] 2.05Å' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2zbj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Macropsychanthus_bicolor Macropsychanthus bicolor]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZBJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZBJ FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.05Å</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=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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=2zbj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zbj OCA], [https://pdbe.org/2zbj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zbj RCSB], [https://www.ebi.ac.uk/pdbsum/2zbj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zbj ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/LECA_DIORO LECA_DIORO] D-mannose/D-glucose-binding lectin. Induces histamine release in mast cells from hamster and rat. Induces lymphocyte proliferation and IFNG production.<ref>PMID:18682294</ref> <ref>PMID:1398779</ref> <ref>PMID:7524287</ref> <ref>PMID:8891754</ref> <ref>PMID:9575151</ref> <ref>PMID:10747944</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/zb/2zbj_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=2zbj ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The legume lectins from the subtribe Diocleinae, often referred to as concanavalin A-like lectins, are a typical example of highly similar proteins that show distinct biological activities. The pH-dependent oligomerization that some of these lectins undergo and the relative position of amino acids within the carbohydrate-binding site are factors that have been reported to contribute to these differences in the activities of Diocleinae lectins. In the present work, we determined the amino acid sequence and the crystal structure of the lectin of Dioclea rostrata seeds (DRL), with the aim of investigating the structural bases of the different behavior displayed by this lectin in comparison to other Diocleinae lectins and determining the reason for the distinct pH-dependent dimer-tetramer equilibrium. In addition, we discovered a novel multimeric arrangement for this lectin. | |||
Crystal structure of Dioclea rostrata lectin: insights into understanding the pH-dependent dimer-tetramer equilibrium and the structural basis for carbohydrate recognition in Diocleinae lectins.,de Oliveira TM, Delatorre P, da Rocha BA, de Souza EP, Nascimento KS, Bezerra GA, Moura TR, Benevides RG, Bezerra EH, Moreno FB, Freire VN, de Azevedo WF Jr, Cavada BS J Struct Biol. 2008 Nov;164(2):177-82. Epub 2008 Jul 22. PMID:18682294<ref>PMID:18682294</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2zbj" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | [[Category: Large Structures]] | ||
[[Category: Macropsychanthus bicolor]] | |||
[[Category: Benevides RG]] | |||
== | [[Category: Bezerra EHS]] | ||
[[Category: Bezerra GA]] | |||
[[Category: | [[Category: Cavada BS]] | ||
[[Category: | [[Category: Delatorre P]] | ||
[[Category: Benevides | [[Category: Freire VN]] | ||
[[Category: Bezerra | [[Category: Moreno FBMB]] | ||
[[Category: Bezerra | [[Category: Moura TR]] | ||
[[Category: Cavada | [[Category: Nascimento KS]] | ||
[[Category: Delatorre | [[Category: Da Rocha BAM]] | ||
[[Category: Freire | [[Category: De Azevedo Jr WF]] | ||
[[Category: De Oliveira TM]] | |||
[[Category: Moreno | [[Category: De Sousa EP]] | ||
[[Category: Moura | |||
[[Category: Nascimento | |||
[[Category: Rocha | |||
[[Category: | |||
[[Category: | |||
[[Category: | |||
Latest revision as of 16:30, 1 November 2023
Crystal structure of Dioclea rostrata lectinCrystal structure of Dioclea rostrata lectin
Structural highlights
FunctionLECA_DIORO D-mannose/D-glucose-binding lectin. Induces histamine release in mast cells from hamster and rat. Induces lymphocyte proliferation and IFNG production.[1] [2] [3] [4] [5] [6] 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 PubMedThe legume lectins from the subtribe Diocleinae, often referred to as concanavalin A-like lectins, are a typical example of highly similar proteins that show distinct biological activities. The pH-dependent oligomerization that some of these lectins undergo and the relative position of amino acids within the carbohydrate-binding site are factors that have been reported to contribute to these differences in the activities of Diocleinae lectins. In the present work, we determined the amino acid sequence and the crystal structure of the lectin of Dioclea rostrata seeds (DRL), with the aim of investigating the structural bases of the different behavior displayed by this lectin in comparison to other Diocleinae lectins and determining the reason for the distinct pH-dependent dimer-tetramer equilibrium. In addition, we discovered a novel multimeric arrangement for this lectin. Crystal structure of Dioclea rostrata lectin: insights into understanding the pH-dependent dimer-tetramer equilibrium and the structural basis for carbohydrate recognition in Diocleinae lectins.,de Oliveira TM, Delatorre P, da Rocha BA, de Souza EP, Nascimento KS, Bezerra GA, Moura TR, Benevides RG, Bezerra EH, Moreno FB, Freire VN, de Azevedo WF Jr, Cavada BS J Struct Biol. 2008 Nov;164(2):177-82. Epub 2008 Jul 22. PMID:18682294[7] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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