8h62: Difference between revisions
New page: '''Unreleased structure''' The entry 8h62 is ON HOLD until Paper Publication Authors: Description: Category: Unreleased Structures |
No edit summary |
||
| (One intermediate revision by the same user not shown) | |||
| Line 1: | Line 1: | ||
==Crystal structure of Internalin A from Listeria monocytogenes with human E-cadherin EC12== | |||
<StructureSection load='8h62' size='340' side='right'caption='[[8h62]], [[Resolution|resolution]] 1.91Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8h62]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Listeria_monocytogenes_EGD-e Listeria monocytogenes EGD-e]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8H62 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8H62 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]] 1.91Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</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=8h62 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8h62 OCA], [https://pdbe.org/8h62 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8h62 RCSB], [https://www.ebi.ac.uk/pdbsum/8h62 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8h62 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/INLA_LISMO INLA_LISMO] Mediates the entry of L.monocytogenes into cells. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Listeriosis, caused by infection with Listeria monocytogenes, is a severe disease with a high mortality rate. The L. monocytogenes virulence factor, internalin family protein InlA, which binds to the host receptor E-cadherin, is necessary to invade host cells. Here, we isolated two single-domain antibodies (V(H)Hs) that bind to InlA with picomolar affinities from an alpaca immune library using the phage display method. These InlA-specific V(H)Hs inhibited the binding of InlA to the extracellular domains of E-cadherin in vitro as shown by biophysical interaction analysis. Furthermore, we determined that the V(H)Hs inhibited the invasion of L. monocytogenes into host cells in culture. High-resolution X-ray structure analyses of the complexes of V(H)Hs with InlA revealed that the V(H)Hs bind to the same binding site as E-cadherin against InlA. We conclude that these V(H)Hs have the potential for use as drugs to treat listeriosis. | |||
Anti-InlA single-domain antibodies that inhibit the cell invasion of Listeria monocytogenes.,Yamazaki T, Nagatoishi S, Yamawaki T, Nozawa T, Matsunaga R, Nakakido M, Caaveiro JMM, Nakagawa I, Tsumoto K J Biol Chem. 2023 Sep 14:105254. doi: 10.1016/j.jbc.2023.105254. PMID:37716701<ref>PMID:37716701</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 8h62" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Listeria monocytogenes EGD-e]] | |||
[[Category: Caaveiro JMM]] | |||
[[Category: Nagatoish S]] | |||
[[Category: Tsumoto K]] | |||
Latest revision as of 15:33, 4 October 2023
Crystal structure of Internalin A from Listeria monocytogenes with human E-cadherin EC12Crystal structure of Internalin A from Listeria monocytogenes with human E-cadherin EC12
Structural highlights
FunctionINLA_LISMO Mediates the entry of L.monocytogenes into cells. Publication Abstract from PubMedListeriosis, caused by infection with Listeria monocytogenes, is a severe disease with a high mortality rate. The L. monocytogenes virulence factor, internalin family protein InlA, which binds to the host receptor E-cadherin, is necessary to invade host cells. Here, we isolated two single-domain antibodies (V(H)Hs) that bind to InlA with picomolar affinities from an alpaca immune library using the phage display method. These InlA-specific V(H)Hs inhibited the binding of InlA to the extracellular domains of E-cadherin in vitro as shown by biophysical interaction analysis. Furthermore, we determined that the V(H)Hs inhibited the invasion of L. monocytogenes into host cells in culture. High-resolution X-ray structure analyses of the complexes of V(H)Hs with InlA revealed that the V(H)Hs bind to the same binding site as E-cadherin against InlA. We conclude that these V(H)Hs have the potential for use as drugs to treat listeriosis. Anti-InlA single-domain antibodies that inhibit the cell invasion of Listeria monocytogenes.,Yamazaki T, Nagatoishi S, Yamawaki T, Nozawa T, Matsunaga R, Nakakido M, Caaveiro JMM, Nakagawa I, Tsumoto K J Biol Chem. 2023 Sep 14:105254. doi: 10.1016/j.jbc.2023.105254. PMID:37716701[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||||