View source for 4nun


==Crystal structure of copper-bound Na-ASP-2==
<StructureSection load='4nun' size='340' side='right'caption='[[4nun]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4nun]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Necator_americanus Necator americanus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NUN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NUN 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]] 2.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</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=4nun FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nun OCA], [https://pdbe.org/4nun PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nun RCSB], [https://www.ebi.ac.uk/pdbsum/4nun PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nun ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/J9ULM6_NECAM J9ULM6_NECAM] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Hookworm activation-associated secreted proteins can be structurally classified into at least three different groups. The hallmark feature of Group 1 activation-associated secreted proteins is a prominent equatorial groove, which is inferred to form a ligand binding site. Furthermore, a conserved tandem histidine motif is located in the centre of the groove and believed to provide or support a yet to be determined catalytic activity. Here, we report three-dimensional crystal structures of Na-ASP-2, an L3-secreted activation-associated secreted protein from the human hookworm Necator americanus, which demonstrate transition metal binding ability of the conserved tandem histidine motif. We further identified moderate phosphohydrolase activity of recombinant Na-ASP-2, which relates to the tandem histidine motif. By panning a random 12-mer peptide phage library, we identified a peptide with high similarity to the human calcium-activated potassium channel SK3, and confirm binding of the synthetic peptide to recombinant Na-ASP-2 by differential scanning fluorimetry. Potential binding modes of the peptide to Na-ASP-2 were studied by molecular dynamics simulations which clearly identify a preferred topology of the Na-ASP-2:SK3 peptide complex.

Probing the equatorial groove of the hookworm protein and vaccine candidate antigen, Na-ASP-2.,Mason L, Tribolet L, Simon A, von Gnielinski N, Nienaber L, Taylor P, Willis C, Jones MK, Sternberg PW, Gasser RB, Loukas A, Hofmann A Int J Biochem Cell Biol. 2014 May;50:146-55. doi: 10.1016/j.biocel.2014.03.003., Epub 2014 Mar 13. PMID:24631931<ref>PMID:24631931</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4nun" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Necator americanus]]
[[Category: Hofmann A]]