3s5x

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Current revision (12:47, 14 March 2024) (edit) (undo)
 
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<StructureSection load='3s5x' size='340' side='right'caption='[[3s5x]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
<StructureSection load='3s5x' size='340' side='right'caption='[[3s5x]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3s5x]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"planktothrix_agardhii"_emend._suda_et_al._2002 "planktothrix agardhii" emend. suda et al. 2002]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3S5X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3S5X FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3s5x]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Planktothrix_agardhii Planktothrix agardhii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3S5X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3S5X FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.65&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3s5v|3s5v]], [[3obl|3obl]], [[3s60|3s60]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">OAA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1160 "Planktothrix agardhii" emend. Suda et al. 2002])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3s5x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s5x OCA], [https://pdbe.org/3s5x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3s5x RCSB], [https://www.ebi.ac.uk/pdbsum/3s5x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3s5x ProSAT]</span></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=3s5x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s5x OCA], [https://pdbe.org/3s5x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3s5x RCSB], [https://www.ebi.ac.uk/pdbsum/3s5x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3s5x ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/LEC1_PLAAG LEC1_PLAAG] Lectin specific for high mannose N-glycans, recognizes the branched moiety of these glycans. Does not recognize other types of N-glycans or monosaccharides. Agglutinates trypsin-treated rabbit erythrocytes. Does not require divalent cations for activity. Inhibits HIV replication in MT4 cells with an EC(50) of 45 nM. Binds to the HIV envelope glycoprotein gp120.<ref>PMID:10817903</ref> <ref>PMID:17314091</ref>
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The cyanobacterial Oscillatory Agardhii agglutinin (OAA) is a recently discovered HIV-inactivating lectin that interacts with high-mannose sugars. Nuclear magnetic resonance (NMR) binding studies between OAA and alpha3,alpha6-mannopentaose (Manalpha(1-3)[Manalpha(1-3)[Manalpha(1-6)]Manalpha(1-6)]Man), the branched core unit of Man-9, revealed two binding sites at opposite ends of the protein, exhibiting essentially identical affinities. Atomic details of the specific protein-sugar contacts in the recognition loops of OAA were delineated in the high-resolution crystal structures of free and glycan-complexed protein. No major changes in the overall protein structure are induced by carbohydrate binding, with essentially identical apo- and sugar-bound conformations in binding site 1. A single peptide bond flip at W77-G78 is seen in binding site 2. Our combined NMR and crystallographic results provide structural insights into the mechanism by which OAA specifically recognizes the branched Man-9 core, distinctly different from the recognition of the D1 and D3 arms at the nonreducing end of high-mannose carbohydrates by other antiviral lectins.
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Structural basis of the anti-HIV activity of the cyanobacterial Oscillatoria Agardhii agglutinin.,Koharudin LM, Gronenborn AM Structure. 2011 Aug 10;19(8):1170-81. PMID:21827952<ref>PMID:21827952</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3s5x" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Planktothrix agardhii emend. suda et al. 2002]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Gronenborn, A M]]
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[[Category: Planktothrix agardhii]]
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[[Category: Koharudin, L M.I]]
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[[Category: Gronenborn AM]]
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[[Category: Anti-hiv lectin]]
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[[Category: Koharudin LMI]]
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[[Category: Beta barrel like protein]]
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[[Category: Carbohydrate]]
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[[Category: Protein binding]]
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Current revision

Structure of the cyanobacterial Oscillatoria Agardhii Agglutinin (OAA) in complex with a3,a6 mannopentaose

PDB ID 3s5x

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