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==Structure of human Fibrinogen-like protein 1==
==Structure of the Fibrinogen C-terminal domain of FGL1==
<StructureSection load='7tz2' size='340' side='right'caption='[[7tz2]], [[Resolution|resolution]] 2.55&Aring;' scene=''>
<StructureSection load='7tz2' size='340' side='right'caption='[[7tz2]], [[Resolution|resolution]] 2.55&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[7tz2]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7TZ2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7TZ2 FirstGlance]. <br>
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7TZ2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7TZ2 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]] 2.55&#8491;</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.55&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=7tz2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7tz2 OCA], [https://pdbe.org/7tz2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7tz2 RCSB], [https://www.ebi.ac.uk/pdbsum/7tz2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7tz2 ProSAT]</span></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=7tz2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7tz2 OCA], [https://pdbe.org/7tz2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7tz2 RCSB], [https://www.ebi.ac.uk/pdbsum/7tz2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7tz2 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FGL1_HUMAN FGL1_HUMAN] Immune suppressive molecule that inhibits antigen-specific T-cell activation by acting as a major ligand of LAG3 (PubMed:30580966). Responsible for LAG3 T-cell inhibitory function (PubMed:30580966). Binds LAG3 independently from MHC class II (MHC-II) (PubMed:30580966). Secreted by, and promotes growth of, hepatocytes (PubMed:11470158, PubMed:19880967).<ref>PMID:11470158</ref> <ref>PMID:19880967</ref> <ref>PMID:30580966</ref>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The immune checkpoint receptor lymphocyte activation gene 3 protein (LAG3) inhibits T cell function upon binding to major histocompatibility complex class II (MHC class II) or fibrinogen-like protein 1 (FGL1). Despite the emergence of LAG3 as a target for next-generation immunotherapies, we have little information describing the molecular structure of the LAG3 protein or how it engages cellular ligands. Here we determined the structures of human and murine LAG3 ectodomains, revealing a dimeric assembly mediated by Ig domain 2. Epitope mapping indicates that a potent LAG3 antagonist antibody blocks interactions with MHC class II and FGL1 by binding to a flexible 'loop 2' region in LAG3 domain 1. We also defined the LAG3-FGL1 interface by mapping mutations onto structures of LAG3 and FGL1 and established that FGL1 cross-linking induces the formation of higher-order LAG3 oligomers. These insights can guide LAG3-based drug development and implicate ligand-mediated LAG3 clustering as a mechanism for disrupting T cell activation.
LAG3 ectodomain structure reveals functional interfaces for ligand and antibody recognition.,Ming Q, Celias DP, Wu C, Cole AR, Singh S, Mason C, Dong S, Tran TH, Amarasinghe GK, Ruffell B, Luca VC Nat Immunol. 2022 Jun 27. pii: 10.1038/s41590-022-01238-7. doi:, 10.1038/s41590-022-01238-7. PMID:35761082<ref>PMID:35761082</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7tz2" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Luca VC]]
[[Category: Luca VC]]
[[Category: Ming Q]]
[[Category: Ming Q]]
[[Category: Tran TH]]
[[Category: Tran TH]]

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