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4uei
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 4uei is ON HOLD until Paper Publication Authors: LIU, X., MA, H., Yan, X., Hong, H., Peng, J., Peng, R. Description: Solution structure of the ster...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Solution structure of the sterol carrier protein domain 2 of Helicoverpa armigera== | |
| + | <StructureSection load='4uei' size='340' side='right'caption='[[4uei]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4uei]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicoverpa_armigera Helicoverpa armigera]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UEI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4UEI FirstGlance]. <br> | ||
| + | </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=4uei FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uei OCA], [https://pdbe.org/4uei PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4uei RCSB], [https://www.ebi.ac.uk/pdbsum/4uei PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4uei ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/K7NSY9_HELAM K7NSY9_HELAM] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The cotton bollworm, Helicoverpa armigera, has developed strong resistance to many insecticides. Sterol Carrier Protein-2 (SCP-2) is an important non-specific lipid transfer protein in insects and appears to be a potential new target. In order to elucidate the structure and function of Helicoverpa armigera SCP-2 (HaSCP-2), NMR spectroscopy, docking simulations, mutagenesis and bioassays were performed. HaSCP-2 composed of five alpha-helices and four stranded beta-sheets. The folds of alpha-helices and beta-sheets interacted together to form a hydrophobic cavity with putative entrance and exit openings, which served as a tunnel for accommodating and transporting of lipids. Several sterols and fatty acids could interact with HaSCP-2 via important hydrophobic sites, which could be potential targets for insecticides. Mutagenesis experiments indicated Y51, F53, F89, F110, I117 and Q131 may be the key functional sites. HaSCP-2 showed high cholesterol binding activity and SCP-2 inhibitors (SCPIs) could inhibit the biological activity of HaSCP-2. SCPI-treated larvae at young stage showed a significant decrease of cholesterol uptake in vivo. Our study describes for the first time a NMR structure of SCP-2 in lepidopteran H. armigera and reveals its important function in cholesterol uptake, which facilitates the screening of effective insecticides targeting the insect cholesterol metabolism. | ||
| - | + | NMR structure and function of Helicoverpa armigera sterol carrier protein-2, an important insecticidal target from the cotton bollworm.,Ma H, Ma Y, Liu X, Dyer DH, Xu P, Liu K, Lan Q, Hong H, Peng J, Peng R Sci Rep. 2015 Dec 10;5:18186. doi: 10.1038/srep18186. PMID:26655641<ref>PMID:26655641</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 4uei" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Helicoverpa armigera]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Hong H]] | ||
| + | [[Category: Liu X]] | ||
| + | [[Category: Ma H]] | ||
| + | [[Category: Peng J]] | ||
| + | [[Category: Peng R]] | ||
| + | [[Category: Yan X]] | ||
Current revision
Solution structure of the sterol carrier protein domain 2 of Helicoverpa armigera
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Categories: Helicoverpa armigera | Large Structures | Hong H | Liu X | Ma H | Peng J | Peng R | Yan X
