7wkf: Difference between revisions
From Proteopedia
Jump to navigationJump to search
m Protected "7wkf" [edit=sysop:move=sysop] |
No edit summary |
||
| Line 1: | Line 1: | ||
The | ==Antimicrobial peptide-LaIT2== | ||
<StructureSection load='7wkf' size='340' side='right'caption='[[7wkf]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7wkf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Liocheles_australasiae Liocheles australasiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7WKF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7WKF 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=7wkf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7wkf OCA], [https://pdbe.org/7wkf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7wkf RCSB], [https://www.ebi.ac.uk/pdbsum/7wkf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7wkf ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/KBX2_LIOAU KBX2_LIOAU] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
LaIT2, composed of 59 amino acid residues, is a peptide toxin isolated from the venom of the Yaeyama scorpion, Liocheles australasiae. LaIT2 is toxic to insects but not most mammals. The N- and C-domains of LaIT2 are known to possess antimicrobial and insecticidal activities, respectively. However, the molecular mechanisms are largely unknown because of the lack of a three-dimensional structure of LaIT2. Thus, we elucidated the solution NMR structure of LaIT2. LaIT2 adopts a beta-KTx-like two-domain structure, in which the N- and C-terminal domains form a random coil and an alpha-beta-beta motif, respectively. Trifluoro ethanol and liposomes titration experiments showed that the unstructured N-domain of LaIT2 has the ability to form an alpha-helix. The N-terminal helix is amphiphilic, and one side of the helix is positively charged. Measurements of the antimicrobial and insecticidal activities of LaIT2 mutants suggested K15 in the N-domain was found to be responsible for the antimicrobial activities, whereas L53 and L54 in the C-domain were key residues involved in the insecticidal activity. Moreover, K21 in the N-domain is important for both activities. Therefore, two domains are suggested that they work together to show antimicrobial and insecticidal activity. | |||
Structural and functional studies of LaIT2, an antimicrobial and insecticidal peptide from Liocheles australasiae.,Tamura M, Tatsushiro C, Morita EH, Ohki S Toxicon. 2022 Jul 30;214:8-17. doi: 10.1016/j.toxicon.2022.04.015. Epub 2022 Apr , 29. PMID:35490851<ref>PMID:35490851</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 7wkf" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Liocheles australasiae]] | |||
[[Category: Morita H]] | |||
[[Category: Ohki S]] | |||
[[Category: Tamura M]] | |||
Latest revision as of 06:23, 7 April 2023
Antimicrobial peptide-LaIT2
| ||||||||||||
