View source for 3uqi


==Crystallographic structure of FKBP12 from Aedes aegypti==
<StructureSection load='3uqi' size='340' side='right'caption='[[3uqi]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3uqi]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aedes_aegypti Aedes aegypti]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UQI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UQI 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]] 1.302&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MPO:3[N-MORPHOLINO]PROPANE+SULFONIC+ACID'>MPO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=3uqi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uqi OCA], [https://pdbe.org/3uqi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3uqi RCSB], [https://www.ebi.ac.uk/pdbsum/3uqi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3uqi ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q1HR83_AEDAE Q1HR83_AEDAE] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Dengue is one of the most infectious viral diseases prevalent mainly in tropical countries. The virus is transmitted by Aedes species of mosquito, primarily Aedes aegypti. Dengue remains a challenging drug target for years as the virus eludes the immune responses. Currently, no vaccines or antiviral drugs are available for dengue prevention. Previous studies suggested that the immunosuppressive drug FK506 shows antimalarial activity, and its molecular target, FK506-binding protein (FKBP), was identified in the Plasmodium parasite. Likewise, a FKBP family protein has been identified in A. aegypti (AaFKBP12) in which AaFKBP12 is assumed to play a similar role in its life cycle. FKBPs belong to a highly conserved class of proteins and are considered as an attractive pharmacological target. Herein, we present a high-resolution crystal structure of AaFKBP12 at 1.3 A resolution and discuss its structural features throwing light in facilitating the design of potential antagonists against the dengue-transmitting mosquito.

High-resolution crystal structure of FKBP12 from Aedes aegypti.,Rajan S, Saw KQ, Nguyen QT, Baek K, Yoon HS Protein Sci. 2012 Jul;21(7):1080-4. doi: 10.1002/pro.2079. Epub 2012 May 18. PMID:22517662<ref>PMID:22517662</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3uqi" style="background-color:#fffaf0;"></div>

==See Also==
*[[FKBP 3D structures|FKBP 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Aedes aegypti]]
[[Category: Large Structures]]
[[Category: Saw KQ]]
[[Category: Sreekanth R]]
[[Category: Yoon HS]]