4bqu: Difference between revisions
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==Japanin from Rhipicephalus appendiculatus bound to cholesterol: Orthorhombic crystal form== | ==Japanin from Rhipicephalus appendiculatus bound to cholesterol: Orthorhombic crystal form== | ||
<StructureSection load='4bqu' size='340' side='right' caption='[[4bqu]], [[Resolution|resolution]] 2.36Å' scene=''> | <StructureSection load='4bqu' size='340' side='right'caption='[[4bqu]], [[Resolution|resolution]] 2.36Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4bqu]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BQU OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[4bqu]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhipicephalus_appendiculatus Rhipicephalus appendiculatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BQU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BQU FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CLR:CHOLESTEROL'>CLR</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand= | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.36Å</td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CLR:CHOLESTEROL'>CLR</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | ||
<table> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4bqu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bqu OCA], [https://pdbe.org/4bqu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bqu RCSB], [https://www.ebi.ac.uk/pdbsum/4bqu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bqu ProSAT]</span></td></tr> | ||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/JAP_RHIAP JAP_RHIAP] Salivary tick protein that modulates host immune response. This protein blocks dendritic cell (DC) differentiation from monocytes (PubMed:23825947). In addition, it inhibits up-regulation of costimulatory molecules and pro-inflammatory cytokines in response to stimuli and promotes up-regulation of co-inhibitory molecules and the anti-inflammatory cytokine interleukin-10 (PubMed:23825947). It has a pocket to accomodate cholesterol, which may have immune-modulatory roles, either directly or through interactions with the host gut microbiota (Probable).<ref>PMID:23825947</ref> <ref>PMID:29167574</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Two crystal structures of Japanin, an 18 kDa immune-modulatory lipocalin from the Brown Ear Tick (Rhipicephalus appendiculatus), have been determined at 2.2 and 2.4 A resolution. In both crystal forms the protein is in complex with cholesterol, which sits in a closed pocket at the centre of the lipocalin barrel. Both crystal forms are dimers, which are also observed in solution. Molecular modelling suggests that previously-described members of a tick protein family bearing high sequence homology to Japanin are also likely to bind cholesterol or cholesterol derivatives. | |||
Structural basis of cholesterol binding by a novel clade of dendritic cell modulators from ticks.,Roversi P, Johnson S, Preston SG, Nunn MA, Paesen GC, Austyn JM, Nuttall PA, Lea SM Sci Rep. 2017 Nov 22;7(1):16057. doi: 10.1038/s41598-017-16413-2. PMID:29167574<ref>PMID:29167574</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4bqu" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Rhipicephalus appendiculatus]] | ||
[[Category: | [[Category: Austyn JM]] | ||
[[Category: | [[Category: Johnson S]] | ||
[[Category: | [[Category: Lea SM]] | ||
[[Category: | [[Category: Nuttall P]] | ||
[[Category: | [[Category: Preston S]] | ||
[[Category: | [[Category: Roversi P]] | ||
Latest revision as of 14:56, 20 December 2023
Japanin from Rhipicephalus appendiculatus bound to cholesterol: Orthorhombic crystal formJapanin from Rhipicephalus appendiculatus bound to cholesterol: Orthorhombic crystal form
Structural highlights
FunctionJAP_RHIAP Salivary tick protein that modulates host immune response. This protein blocks dendritic cell (DC) differentiation from monocytes (PubMed:23825947). In addition, it inhibits up-regulation of costimulatory molecules and pro-inflammatory cytokines in response to stimuli and promotes up-regulation of co-inhibitory molecules and the anti-inflammatory cytokine interleukin-10 (PubMed:23825947). It has a pocket to accomodate cholesterol, which may have immune-modulatory roles, either directly or through interactions with the host gut microbiota (Probable).[1] [2] Publication Abstract from PubMedTwo crystal structures of Japanin, an 18 kDa immune-modulatory lipocalin from the Brown Ear Tick (Rhipicephalus appendiculatus), have been determined at 2.2 and 2.4 A resolution. In both crystal forms the protein is in complex with cholesterol, which sits in a closed pocket at the centre of the lipocalin barrel. Both crystal forms are dimers, which are also observed in solution. Molecular modelling suggests that previously-described members of a tick protein family bearing high sequence homology to Japanin are also likely to bind cholesterol or cholesterol derivatives. Structural basis of cholesterol binding by a novel clade of dendritic cell modulators from ticks.,Roversi P, Johnson S, Preston SG, Nunn MA, Paesen GC, Austyn JM, Nuttall PA, Lea SM Sci Rep. 2017 Nov 22;7(1):16057. doi: 10.1038/s41598-017-16413-2. PMID:29167574[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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