9q1h
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==A7 minibinder in complex with Abp2D== | |
| + | <StructureSection load='9q1h' size='340' side='right'caption='[[9q1h]], [[Resolution|resolution]] 1.35Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[9q1h]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Acinetobacter_baumannii_ACICU Acinetobacter baumannii ACICU] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9Q1H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9Q1H 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]] 1.35Å</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=9q1h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9q1h OCA], [https://pdbe.org/9q1h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9q1h RCSB], [https://www.ebi.ac.uk/pdbsum/9q1h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9q1h ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A0A7U3Y091_ACIBC A0A7U3Y091_ACIBC] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The rise of multidrug-resistant bacterial infections necessitates the discovery of novel antimicrobial strategies. Here, we show that protein design provides a generalizable means of generating new antimicrobials by neutralizing the function of bacterial adhesins, which are virulence factors critical in host-pathogen interactions. We de novo designed high-affinity miniprotein binders to FimH and Abp1D/Abp2D chaperone usher pili adhesins from uropathogenic Escherichia coli and Acinetobacter baumannii, respectively, which are implicated in mediating both uncomplicated and catheter-associated urinary tract infections (UTI) responsible for significant morbidity and mortality worldwide. The designed antagonists have high specificity and stability, disrupt bacterial recognition of host receptors, block biofilm formation, and are effective in treating and preventing uncomplicated and catheter-associated UTIs in vivo. Targeting virulence factors outside the cell membrane with protein design provides a rapid route to next-generation therapeutics that can disrupt pathogenesis and thus are capable of treating and preventing disease in an antibiotic-sparing manner. | ||
| - | + | De Novo Design of Miniprotein Inhibitors of Bacterial Adhesins.,Chazin-Gray AM, Thompson TR, Lopatto EDB, Magala P, Erickson PW, Hunt AC, Manchenko A, Aprikian P, Tchesnokova V, Basova I, Sanick DA, Tamadonfar KO, Timm MR, Pinkner JS, Dodson KW, Kang A, Joyce E, Bera AK, Schmitz AJ, Ellebedy AH, Hvorecny KL, Cartwright MJ, Vernet A, Bardales S, White D, Klevit RE, Sokurenko EV, Hultgren SJ, Baker D bioRxiv [Preprint]. 2025 Aug 18:2025.08.18.670751. doi: , 10.1101/2025.08.18.670751. PMID:40894640<ref>PMID:40894640</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 9q1h" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Acinetobacter baumannii ACICU]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Synthetic construct]] | ||
| + | [[Category: Hultgren SJ]] | ||
| + | [[Category: Lopatto EDB]] | ||
| + | [[Category: Tamadonfar KO]] | ||
Current revision
A7 minibinder in complex with Abp2D
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