4gu8: Difference between revisions
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==Crystal Structure of Burkholderia oklahomensis agglutinin (BOA)== | |||
=== | <StructureSection load='4gu8' size='340' side='right' caption='[[4gu8]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4gu8]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Burkholderia_oklahomensis Burkholderia oklahomensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GU8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GU8 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DTT:2,3-DIHYDROXY-1,4-DITHIOBUTANE'>DTT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4gk9|4gk9]]</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=4gu8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gu8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4gu8 RCSB], [http://www.ebi.ac.uk/pdbsum/4gu8 PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Burkholderia oklahomensis EO147 agglutinin (BOA) is a 29 kDa member of the Oscillatoria agardhii agglutinin (OAA) family of lectins. Members of the OAA family recognize high-mannose glycans, and, by binding to the HIV envelope glycoprotein 120 (gp120), block the virus from binding to and entering the host cell, thereby inhibiting infection. OAA-family lectins comprise either one or two homologous domains, with a single domain possessing two glycan binding sites. We solved the structure of BOA in the ligand-free form as well as in complex with four molecules of 3alpha,6alpha-mannopentaose, the core unit of the N-linked high-mannose structures found on gp120 in vivo. This is the first structure of a double-domain OAA-family lectin in which all four binding sites are occupied by ligand. The structural details of the BOA-glycan interactions presented here, together with determination of affinity constants and HIV inactivation data, shed further light onto the structure-function relationship in this important class of anti-HIV proteins. | |||
Burkholderia oklahomensis agglutinin is a canonical two-domain OAA-family lectin: structures, carbohydrate binding and anti-HIV activity.,Whitley MJ, Furey W, Kollipara S, Gronenborn AM FEBS J. 2013 May;280(9):2056-67. doi: 10.1111/febs.12229. Epub 2013 Apr 2. PMID:23480609<ref>PMID:23480609</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Burkholderia oklahomensis]] | [[Category: Burkholderia oklahomensis]] | ||
[[Category: Furey, W | [[Category: Furey, W]] | ||
[[Category: Gronenborn, A M | [[Category: Gronenborn, A M]] | ||
[[Category: Whitley, M J | [[Category: Whitley, M J]] | ||
[[Category: Anti-hiv]] | [[Category: Anti-hiv]] | ||
[[Category: Beta barrel]] | [[Category: Beta barrel]] | ||
Revision as of 14:48, 21 December 2014
Crystal Structure of Burkholderia oklahomensis agglutinin (BOA)Crystal Structure of Burkholderia oklahomensis agglutinin (BOA)
Structural highlights
Publication Abstract from PubMedBurkholderia oklahomensis EO147 agglutinin (BOA) is a 29 kDa member of the Oscillatoria agardhii agglutinin (OAA) family of lectins. Members of the OAA family recognize high-mannose glycans, and, by binding to the HIV envelope glycoprotein 120 (gp120), block the virus from binding to and entering the host cell, thereby inhibiting infection. OAA-family lectins comprise either one or two homologous domains, with a single domain possessing two glycan binding sites. We solved the structure of BOA in the ligand-free form as well as in complex with four molecules of 3alpha,6alpha-mannopentaose, the core unit of the N-linked high-mannose structures found on gp120 in vivo. This is the first structure of a double-domain OAA-family lectin in which all four binding sites are occupied by ligand. The structural details of the BOA-glycan interactions presented here, together with determination of affinity constants and HIV inactivation data, shed further light onto the structure-function relationship in this important class of anti-HIV proteins. Burkholderia oklahomensis agglutinin is a canonical two-domain OAA-family lectin: structures, carbohydrate binding and anti-HIV activity.,Whitley MJ, Furey W, Kollipara S, Gronenborn AM FEBS J. 2013 May;280(9):2056-67. doi: 10.1111/febs.12229. Epub 2013 Apr 2. PMID:23480609[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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