3s64 | pdb_00003s64

Saposin-like protein Ac-SLP-1

spinqualitylabelsall models 3s64, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3s64 is a 1 chain structure with sequence from Ancylostoma caninum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.301Å Ligands: CIT, EPE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q0MRQ4_ANCCA 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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