View source for 3lhc


==Crystal structure of cyanovirin-n swapping domain b mutant==
<StructureSection load='3lhc' size='340' side='right'caption='[[3lhc]], [[Resolution|resolution]] 1.34&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3lhc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Nostoc_ellipsosporum Nostoc ellipsosporum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LHC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LHC FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.34&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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=3lhc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lhc OCA], [https://pdbe.org/3lhc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3lhc RCSB], [https://www.ebi.ac.uk/pdbsum/3lhc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3lhc ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CVN_NOSEL CVN_NOSEL] Mannose-binding lectin.<ref>PMID:9210678</ref> <ref>PMID:12678493</ref> 
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lh/3lhc_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3lhc ConSurf].
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== Publication Abstract from PubMed ==
Cyanovirin-N (CV-N) is a two-domain, cyanobacterial protein that inhibits human immunodeficiency virus (HIV) at nanomolar concentrations by binding to high mannose sugars on the HIV envelope glycoprotein gp120. The wild type protein can exist as a monomer or a domain-swapped dimer with the monomer and dimer containing two or four sugar binding sites, respectively, one on each domain. Here we demonstrate that monomeric, single binding site mutants are completely inactive and that a single site, whether located on domain A or B, is insufficient to impart the antiviral activity. Linking inactive, monomeric proteins in a head-to-head fashion by an intermolecular disulfide bond or by creating an exclusively domain-swapped dimer via a hinge residue deletion restored antiviral activity to levels similar to that of wild type CV-N. These findings demonstrate unequivocally that multisite binding by CV-N type lectins is necessary for viral inhibition.

Anti-HIV activity of defective cyanovirin-N mutants is restored by dimerization.,Matei E, Zheng A, Furey W, Rose J, Aiken C, Gronenborn AM J Biol Chem. 2010 Apr 23;285(17):13057-65. Epub 2010 Feb 10. PMID:20147291<ref>PMID:20147291</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 3lhc" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Nostoc ellipsosporum]]
[[Category: Aiken C]]
[[Category: Furey W]]
[[Category: Gronenborn AM]]
[[Category: Matei E]]
[[Category: Rose J]]
[[Category: Zheng A]]