2lpv: Difference between revisions
New page: '''Unreleased structure''' The entry 2lpv is ON HOLD Authors: Chakraborty, G., Shin, J. Description: Solution Structure of FKBP12 from Aedes aegypti |
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==Solution Structure of FKBP12 from Aedes aegypti== | |||
<StructureSection load='2lpv' size='340' side='right'caption='[[2lpv]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2lpv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aedes_aegypti Aedes aegypti]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LPV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LPV FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2lpv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lpv OCA], [https://pdbe.org/2lpv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lpv RCSB], [https://www.ebi.ac.uk/pdbsum/2lpv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lpv 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 remains one of the major public concerns as the virus eludes the immune response. Currently, no vaccines or antiviral therapeutics are available for dengue prevention or treatment. Immunosuppressive drug FK506 shows an antimalarial activity, and its molecular target, FK506-binding protein (FKBP), was identified in human Plasmodium parasites. Likewise, a conserved FKBP family protein has also been identified in Aedes aegypti (AaFKBP12), which is expected to play a similar role in the life cycle of Aedes aegypti, the primary vector of dengue virus infection. As FKBPs belong to a highly conserved class of immunophilin family and are involved in key biological regulations, they are considered as attractive pharmacological targets. In this study, we have determined the nuclear magnetic resonance solution structure of AaFKBP12, a novel FKBP member from Aedes aegypti, and presented its structural features, which may facilitate the design of potential inhibitory ligands against the dengue-transmitting mosquitoes. | |||
Solution structure of FK506-binding protein 12 from Aedes aegypti.,Chakraborty G, Shin J, Nguyen QT, Harikishore A, Baek K, Yoon HS Proteins. 2012 Oct;80(10):2476-81. doi: 10.1002/prot.24146. Epub 2012 Jul 31. PMID:22806993<ref>PMID:22806993</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2lpv" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[FKBP 3D structures|FKBP 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Aedes aegypti]] | |||
[[Category: Large Structures]] | |||
[[Category: Chakraborty G]] | |||
[[Category: Shin J]] | |||
Latest revision as of 08:48, 15 May 2024
Solution Structure of FKBP12 from Aedes aegyptiSolution Structure of FKBP12 from Aedes aegypti
Structural highlights
FunctionPublication Abstract from PubMedDengue remains one of the major public concerns as the virus eludes the immune response. Currently, no vaccines or antiviral therapeutics are available for dengue prevention or treatment. Immunosuppressive drug FK506 shows an antimalarial activity, and its molecular target, FK506-binding protein (FKBP), was identified in human Plasmodium parasites. Likewise, a conserved FKBP family protein has also been identified in Aedes aegypti (AaFKBP12), which is expected to play a similar role in the life cycle of Aedes aegypti, the primary vector of dengue virus infection. As FKBPs belong to a highly conserved class of immunophilin family and are involved in key biological regulations, they are considered as attractive pharmacological targets. In this study, we have determined the nuclear magnetic resonance solution structure of AaFKBP12, a novel FKBP member from Aedes aegypti, and presented its structural features, which may facilitate the design of potential inhibitory ligands against the dengue-transmitting mosquitoes. Solution structure of FK506-binding protein 12 from Aedes aegypti.,Chakraborty G, Shin J, Nguyen QT, Harikishore A, Baek K, Yoon HS Proteins. 2012 Oct;80(10):2476-81. doi: 10.1002/prot.24146. Epub 2012 Jul 31. PMID:22806993[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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