1m9s

<table><tr><td colspan='2'>[[1m9s]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacterium_monocytogenes_hominis"_nyfeldt_1932 "bacterium monocytogenes hominis" nyfeldt 1932]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M9S OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1M9S FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TB:TERBIUM(III)+ION'>TB</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1d0b|1d0b]], [[1h6t|1h6t]], [[1h6u|1h6u]], [[1cka|1cka]], [[2abl|2abl]]</div></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">inlB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1639 "Bacterium monocytogenes hominis" Nyfeldt 1932])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1m9s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m9s OCA], [http://pdbe.org/1m9s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1m9s RCSB], [http://www.ebi.ac.uk/pdbsum/1m9s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1m9s ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/INLB_LISMO INLB_LISMO]] Mediates the entry of Listeria monocytogenes into cells.

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== Publication Abstract from PubMed ==

InlB, a surface-localized protein of Listeria monocytogenes, induces phagocytosis in non-phagocytic mammalian cells by activating Met, a receptor tyrosine kinase. InlB also binds glycosaminoglycans and the protein gC1q-R, two additional host ligands implicated in invasion. We present the structure of InlB, revealing a highly elongated molecule with leucine-rich repeats that bind Met at one end, and GW domains that dissociably bind the bacterial surface at the other. Surprisingly, the GW domains are seen to resemble SH3 domains. Despite this, GW domains are unlikely to act as functional mimics of SH3 domains since their potential proline-binding sites are blocked or destroyed. However, we do show that the GW domains, in addition to binding glycosaminoglycans, bind gC1q-R specifically, and that this binding requires release of InlB from the bacterial surface. Dissociable attachment to the bacterial surface via the GW domains may be responsible for restricting Met activation to a small, localized area of the host cell and for coupling InlB-induced host membrane dynamics with bacterial proximity during invasion.

GW domains of the Listeria monocytogenes invasion protein InlB are SH3-like and mediate binding to host ligands.,Marino M, Banerjee M, Jonquieres R, Cossart P, Ghosh P EMBO J. 2002 Nov 1;21(21):5623-34. PMID:12411480<ref>PMID:12411480</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1m9s" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Bacterium monocytogenes hominis nyfeldt 1932]]

[[Category: Banerjee, M]]

[[Category: Cossart, P]]

[[Category: Ghosh, P]]

[[Category: Jonquieres, R]]

[[Category: Marino, M]]

[[Category: Signaling protein]]