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3q2c

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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)

Structural highlights

3q2c is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.5Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3q2c"

@@ Line 4: / Line 4: @@
 == Structural highlights ==
 <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"><div style='overflow: auto; max-height: 3em;'>[[1vdg|1vdg]]</div></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]] 2.5&#8491;</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>
 == Function ==
-[[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>
+[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;">
 == Publication Abstract from PubMed ==
@@ Line 27: / Line 27: @@
 [[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Chen, Y]]
+[[Category: Chen Y]]
-[[Category: Cheng, H]]
+[[Category: Cheng H]]
-[[Category: Gao, G F]]
+[[Category: Gao GF]]
-[[Category: Liu, J]]
+[[Category: Liu J]]
-[[Category: Qi, J X]]
+[[Category: Qi JX]]
-[[Category: Ryu, M]]
+[[Category: Ryu M]]
-[[Category: Shi, Y]]
+[[Category: Shi Y]]
-[[Category: Activating receptor]]
-[[Category: Hla binding]]
-[[Category: Ilt6]]
-[[Category: Immune system]]
-[[Category: Lilra3]]

3q2c

From Proteopedia

Current revision

Binding properties to HLA class I molecules and the structure of the leukocyte Ig-like receptor A3 (LILRA3/ILT6/LIR4/CD85e)

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

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