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| | ==Binding properties to HLA class I molecules and the structure of the leukocyte Ig-like receptor A3 (LILRA3/ILT6/LIR4/CD85e)== | | ==Binding properties to HLA class I molecules and the structure of the leukocyte Ig-like receptor A3 (LILRA3/ILT6/LIR4/CD85e)== |
| - | <StructureSection load='3q2c' size='340' side='right' caption='[[3q2c]], [[Resolution|resolution]] 2.50Å' scene=''> | + | <StructureSection load='3q2c' size='340' side='right'caption='[[3q2c]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3q2c]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3Q2C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3Q2C FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3q2c]] is a 1 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=3Q2C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3Q2C FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1vdg|1vdg]]</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]] 2.5Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3q2c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q2c OCA], [http://pdbe.org/3q2c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3q2c RCSB], [http://www.ebi.ac.uk/pdbsum/3q2c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3q2c 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=3q2c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q2c OCA], [https://pdbe.org/3q2c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3q2c RCSB], [https://www.ebi.ac.uk/pdbsum/3q2c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3q2c ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/LIRA3_HUMAN LIRA3_HUMAN]] Acts as soluble receptor for class I MHC antigens. Binds both classical and non-classical HLA class I molecules but with reduced affinities compared to LILRB1 or LILRB2. Binds with high affinity to the surface of monocytes, leading to abolish LPS-induced TNF-alpha production by monocytes.<ref>PMID:21559424</ref> <ref>PMID:24085305</ref> | + | [https://www.uniprot.org/uniprot/LIRA3_HUMAN LIRA3_HUMAN] Acts as soluble receptor for class I MHC antigens. Binds both classical and non-classical HLA class I molecules but with reduced affinities compared to LILRB1 or LILRB2. Binds with high affinity to the surface of monocytes, leading to abolish LPS-induced TNF-alpha production by monocytes.<ref>PMID:21559424</ref> <ref>PMID:24085305</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 3q2c" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 3q2c" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Leukocyte immunoglobulin-like receptor|Leukocyte immunoglobulin-like receptor]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Homo sapiens]] | | [[Category: Homo sapiens]] |
| - | [[Category: Chen, Y]] | + | [[Category: Large Structures]] |
| - | [[Category: Cheng, H]] | + | [[Category: Chen Y]] |
| - | [[Category: Gao, G F]] | + | [[Category: Cheng H]] |
| - | [[Category: Liu, J]] | + | [[Category: Gao GF]] |
| - | [[Category: Qi, J X]] | + | [[Category: Liu J]] |
| - | [[Category: Ryu, M]] | + | [[Category: Qi JX]] |
| - | [[Category: Shi, Y]] | + | [[Category: Ryu M]] |
| - | [[Category: Activating receptor]]
| + | [[Category: Shi Y]] |
| - | [[Category: Hla binding]]
| + | |
| - | [[Category: Ilt6]]
| + | |
| - | [[Category: Immune system]]
| + | |
| - | [[Category: Lilra3]]
| + | |
| Structural highlights
Function
LIRA3_HUMAN Acts as soluble receptor for class I MHC antigens. Binds both classical and non-classical HLA class I molecules but with reduced affinities compared to LILRB1 or LILRB2. Binds with high affinity to the surface of monocytes, leading to abolish LPS-induced TNF-alpha production by monocytes.[1] [2]
Publication Abstract from PubMed
Structurally, Group 1 LILR (Leukocyte Immunoglobulin (Ig)-Like Receptor, also known as Ig-like transcripts, ILT; Leukocyte Ig-like receptor, LIR; and CD85) members are very similar in terms of the HLAIs (human leukocyte antigen class I molecules) binding region and were hypothesized that they all bind to HLAIs. As one of the Group 1 LILRs, LILRA3 is the only secretory LILR and may greatly control the inhibitory immune response induced by LILRB1, LILRB2, and other HLA-binding LILR molecules like LILRA1. Nevertheless, little was known about the binding of LILRA3 to HLAIs. In this report, we present the crystal structure of the LILRA3 domain 1 (D1) and evaluate the D1 and D1D2 (domain 1 and domain 2) binding to classical and non-classical HLAIs using BIAcore(R) surface plasmon resonance analysis (SPR). We found that LILRA3 binds both classical HLA-A*0201 and non-classical HLA-G1 but with reduced affinities compared to either LILRB1 or LILRB2. The polymorphic amino acids and the LILRA3 D1 structure support this notion.
LILRA3 binds both classical and non-classical HLA class I molecules but with reduced affinities compared to LILRB1/LILRB2: structural evidence.,Ryu M, Chen Y, Qi J, Liu J, Fan Z, Nam G, Shi Y, Cheng H, Gao GF PLoS One. 2011 Apr 29;6(4):e19245. PMID:21559424[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ryu M, Chen Y, Qi J, Liu J, Fan Z, Nam G, Shi Y, Cheng H, Gao GF. LILRA3 binds both classical and non-classical HLA class I molecules but with reduced affinities compared to LILRB1/LILRB2: structural evidence. PLoS One. 2011 Apr 29;6(4):e19245. PMID:21559424 doi:10.1371/journal.pone.0019245
- ↑ Lee TH, Mitchell A, Liu Lau S, An H, Rajeaskariah P, Wasinger V, Raftery M, Bryant K, Tedla N. Glycosylation in a mammalian expression system is critical for the production of functionally active leukocyte immunoglobulin-like receptor A3 protein. J Biol Chem. 2013 Nov 15;288(46):32873-85. doi: 10.1074/jbc.M113.478578. Epub, 2013 Sep 30. PMID:24085305 doi:http://dx.doi.org/10.1074/jbc.M113.478578
- ↑ Ryu M, Chen Y, Qi J, Liu J, Fan Z, Nam G, Shi Y, Cheng H, Gao GF. LILRA3 binds both classical and non-classical HLA class I molecules but with reduced affinities compared to LILRB1/LILRB2: structural evidence. PLoS One. 2011 Apr 29;6(4):e19245. PMID:21559424 doi:10.1371/journal.pone.0019245
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