5y70
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==NMR structure of KMP11 in DPC micelle== | |
| + | <StructureSection load='5y70' size='340' side='right'caption='[[5y70]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5y70]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Trypanosoma_brucei_brucei Trypanosoma brucei brucei]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Y70 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5Y70 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=5y70 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5y70 OCA], [https://pdbe.org/5y70 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5y70 RCSB], [https://www.ebi.ac.uk/pdbsum/5y70 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5y70 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/KM11_TRYBB KM11_TRYBB] May be involved in the regulation of the cytoskeleton through interaction with the subpellicular microtubules. May be involved in parasite mobility and attachment to the surface of the host cell. Behaves as a strong immunogen during infection (By similarity). | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Kinetoplastid membrane protein-11 (KMP11) is a membrane-associated surface protein of kinetoplastids, which has a strong antigenicity but no mammalian homolog, thus representing a promising vaccine candidate. Here, by CD and NMR, we revealed that in buffer, KMP11 assumes a highly helical conformation without stable tertiary packing. Remarkably, upon interacting with dodecylphosphocholine (DPC) micelle, despite minor changes in secondary structures, KMP11 undergoes rearrangements to form a defined structure. We found that its three-dimensional structure unexpectedly adopts the classic four-helix bundle fold. The surface constituted by the N-/C-termini and conserved loop was characterized to dynamically interact with the polar phase of DPC micelle. Our results provide a structural basis for understanding KMP11 functions and further offer a promising avenue for engineering better vaccines. DATABASE: The structure coordinate of KMP11 in DPC micelle has been deposited in PDB with ID of 5Y70 and the associated NMR data were deposited in BMRB with ID of 36112. | ||
| - | + | Kinetoplastid membrane protein-11 adopts a four-helix bundle fold in DPC micelle.,Lim LZ, Ee S, Fu J, Tan Y, He CY, Song J FEBS Lett. 2017 Nov;591(22):3793-3804. doi: 10.1002/1873-3468.12891. Epub 2017, Nov 11. PMID:29082514<ref>PMID:29082514</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 5y70" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| - | [[Category: | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Trypanosoma brucei brucei]] | ||
| + | [[Category: Lim LZ]] | ||
| + | [[Category: Lu Y]] | ||
| + | [[Category: Song J]] | ||
Current revision
NMR structure of KMP11 in DPC micelle
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