3q2c

From Proteopedia

(Difference between revisions)

Revision as of 02:03, 5 August 2016

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.
Related:	1vdg
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 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 1: / Line 1: @@
 ==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]] 2.50&Aring;' scene=''>
@@ Line 4: / Line 5: @@
 <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>
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1vdg|1vdg]]</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://www.rcsb.org/pdb/explore.do?structureId=3q2c RCSB], [http://www.ebi.ac.uk/pdbsum/3q2c PDBsum]</span></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>
 </table>
+== 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>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 14: / Line 17: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 3q2c" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

3q2c

From Proteopedia

Revision as of 02:03, 5 August 2016

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

References

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Proteopedia Page Contributors and Editors (what is this?)

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