3rs6
From Proteopedia
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- | [[ | + | ==Crystal structure Dioclea virgata lectin in complexed with X-mannose== |
+ | <StructureSection load='3rs6' size='340' side='right' caption='[[3rs6]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[3rs6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Dioclea_virgata Dioclea virgata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RS6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3RS6 FirstGlance]. <br> | ||
+ | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=XMM:(2R,3S,4S,5S,6R)-2-(5-BROMO-4-CHLORO-1H-INDOL-3-YLOXY)-TETRAHYDRO-6-(HYDROXYMETHYL)-2H-PYRAN-3,4,5-TRIOL'>XMM</scene><br> | ||
+ | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3rrd|3rrd]]</td></tr> | ||
+ | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3rs6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rs6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3rs6 RCSB], [http://www.ebi.ac.uk/pdbsum/3rs6 PDBsum]</span></td></tr> | ||
+ | <table> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | The lectin of Dioclea virgata (DvirL), both native and complexed with X-man, was submitted to X-ray diffraction analysis and the crystal structure was compared to that of other Diocleinae lectins in order to better understand differences in biological properties, especially with regard to the ability of lectins to induce nitric oxide (NO) production. An association was observed between the volume of the carbohydrate recognition domain (CRD), the ability to induce NO production and the relative positions of Tyr12, Arg228 and Leu99. Thus, differences in biological activity induced by Diocleinae lectins are related to the configuration of amino acid residues in the carbohydrate binding site and to the structural conformation of subsequent regions capable of influencing site-ligand interactions. In conclusion, the ability of Diocleinae lectins to induce NO production depends on CRD configuration. | ||
- | + | Structure of Dioclea virgata lectin: Relations between carbohydrate binding site and nitric oxide production.,Batista da Nobrega R, Rocha BA, Gadelha CA, Santi-Gadelha T, Pires AF, Assreuy AM, Nascimento KS, Nagano CS, Sampaio AH, Cavada BS, Delatorre P Biochimie. 2011 Dec 16. PMID:22198239<ref>PMID:22198239</ref> | |
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- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | == References == | |
- | + | <references/> | |
- | + | __TOC__ | |
- | + | </StructureSection> | |
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- | == | + | |
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[[Category: Dioclea virgata]] | [[Category: Dioclea virgata]] | ||
[[Category: Alencar, K L.]] | [[Category: Alencar, K L.]] |
Revision as of 04:53, 5 June 2014
Crystal structure Dioclea virgata lectin in complexed with X-mannose
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