2mwh: Difference between revisions
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==NMR solution structure of ligand-free OAA== | ==NMR solution structure of ligand-free OAA== | ||
<StructureSection load='2mwh' size='340' side='right'caption='[[2mwh | <StructureSection load='2mwh' size='340' side='right'caption='[[2mwh]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2mwh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2mwh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Planktothrix_agardhii Planktothrix agardhii]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MWH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MWH FirstGlance]. <br> | ||
</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=2mwh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mwh OCA], [https://pdbe.org/2mwh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mwh RCSB], [https://www.ebi.ac.uk/pdbsum/2mwh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mwh ProSAT]</span></td></tr> | </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=2mwh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mwh OCA], [https://pdbe.org/2mwh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mwh RCSB], [https://www.ebi.ac.uk/pdbsum/2mwh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mwh ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[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> | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Ban | [[Category: Planktothrix agardhii]] | ||
[[Category: Carneiro | [[Category: Ban D]] | ||
[[Category: Griesinger | [[Category: Carneiro MG]] | ||
[[Category: Gronenborn | [[Category: Griesinger C]] | ||
[[Category: Koharudin | [[Category: Gronenborn AM]] | ||
[[Category: Lee | [[Category: Koharudin LM]] | ||
[[Category: Mazur | [[Category: Lee D]] | ||
[[Category: Sabo | [[Category: Mazur A]] | ||
[[Category: Trigo-Mourino | [[Category: Sabo T]] | ||
[[Category: Trigo-Mourino P]] | |||
Revision as of 12:49, 14 June 2023
NMR solution structure of ligand-free OAANMR solution structure of ligand-free OAA
Structural highlights
FunctionLEC1_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.[1] [2] Publication Abstract from PubMedLectins from different sources have been shown to interfere with HIV infection by binding to the sugars of viral-envelope glycoproteins. Three-dimensional atomic structures of a number of HIV-inactivating lectins have been determined, both as free proteins and in glycan-bound forms. However, details on the mechanism of recognition and binding to sugars are elusive. Herein we focus on the anti-HIV lectin OAA from Oscillatoria agardhii: We show that in the absence of sugars in solution, both the sugar-free and sugar-bound protein conformations that were observed in the X-ray crystal structures exist as conformational substates. Our results suggest that glycan recognition occurs by conformational selection within the ground state; this model differs from the popular "excited-state" model. Our findings provide further insight into molecular recognition of the major receptor on the HIV virus by OAA. These details can potentially be used for the optimization and/or development of preventive anti-HIV therapeutics. Sampling of Glycan-Bound Conformers by the Anti-HIV Lectin Oscillatoria agardhii agglutinin in the Absence of Sugar.,Carneiro MG, Koharudin LM, Ban D, Sabo TM, Trigo-Mourino P, Mazur A, Griesinger C, Gronenborn AM, Lee D Angew Chem Int Ed Engl. 2015 Apr 14. doi: 10.1002/anie.201500213. PMID:25873445[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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