View source for 3s64


==Saposin-like protein Ac-SLP-1==
<StructureSection load='3s64' size='340' side='right'caption='[[3s64]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3s64]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ancylostoma_caninum Ancylostoma caninum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3S64 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3S64 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]] 2.301&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</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=3s64 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s64 OCA], [https://pdbe.org/3s64 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3s64 RCSB], [https://www.ebi.ac.uk/pdbsum/3s64 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3s64 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q0MRQ4_ANCCA Q0MRQ4_ANCCA] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Saposin-like proteins (SAPLIPs) from soil-transmitted helminths play pivotal roles in host-pathogen interactions and have a high potential as targets for vaccination against parasitic diseases. We have identified two non-orthologous SAPLIPs from human and dog hookworm, Na-SLP-1 and Ac-SLP-1, and solved their three-dimensional crystal structures. Both proteins share the property of membrane binding as monitored by liposome co-pelleting assays and monolayer adsorption. Neither SAPLIP displayed any significant haemolytic or bactericidal activity. Based on the structural information, as well as the results from monolayer adsorption, we propose models of membrane interactions for both SAPLIPs. Initial membrane contact of the monomeric Na-SLP-1 is most likely by electrostatic interactions between the membrane surface and a prominent basic surface patch. In case of the dimeric Ac-SLP-1, membrane interactions are most likely initiated by a unique tryptophan residue that has previously been implicated in membrane interactions in other SAPLIPs.

Insights into the membrane interactions of the saposin-like proteins Na-SLP-1 and Ac-SLP-1 from human and dog hookworm.,Willis C, Wang CK, Osman A, Simon A, Pickering D, Mulvenna J, Riboldi-Tunicliffe A, Jones MK, Loukas A, Hofmann A PLoS One. 2011;6(10):e25369. Epub 2011 Oct 3. PMID:21991310<ref>PMID:21991310</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3s64" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Ancylostoma caninum]]
[[Category: Large Structures]]
[[Category: Hofmann A]]
[[Category: Jones MK]]
[[Category: Loukas A]]
[[Category: Mulvenna J]]
[[Category: Osman A]]
[[Category: Pickering D]]
[[Category: Riboldi-Tunicliffe A]]
[[Category: Simon A]]
[[Category: Wang CK]]
[[Category: Willis C]]