View source for 4uei


==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&reg;/PubMed&reg;, 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]]