4nui: Difference between revisions
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''' | ==Crystal structure of cobalt-bound Na-ASP-2== | ||
<StructureSection load='4nui' size='340' side='right' caption='[[4nui]], [[Resolution|resolution]] 1.70Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4nui]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NUI OCA]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene><br> | |||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4nuk|4nuk]], [[4nun|4nun]], [[4nuo|4nuo]]</td></tr> | |||
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4nui FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nui OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4nui RCSB], [http://www.ebi.ac.uk/pdbsum/4nui PDBsum]</span></td></tr> | |||
<table> | |||
<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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Hofmann, A.]] | |||
[[Category: Excretory/secretory product]] | |||
[[Category: Scp/tap]] | |||
[[Category: Unknown function]] | |||
