View source for 2mwh


==NMR solution structure of ligand-free OAA==
<StructureSection load='2mwh' size='340' side='right'caption='[[2mwh]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2mwh]] 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 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>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Lectins 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<ref>PMID:25873445</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2mwh" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Planktothrix agardhii emend. suda et al. 2002]]
[[Category: Large Structures]]
[[Category: Ban, D]]
[[Category: Carneiro, M G]]
[[Category: Griesinger, C]]
[[Category: Gronenborn, A M]]
[[Category: Koharudin, L M]]
[[Category: Lee, D]]
[[Category: Mazur, A]]
[[Category: Sabo, T]]
[[Category: Trigo-Mourino, P]]
[[Category: Protein binding]]
[[Category: Sugar binding protein-antiviral protein complex]]