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6k60

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'''Unreleased structure'''
 
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The entry 6k60 is ON HOLD until May 31 2021
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==Structural and functional basis for HLA-G isoform recognition of immune checkpoint receptor LILRBs==
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<StructureSection load='6k60' size='340' side='right'caption='[[6k60]], [[Resolution|resolution]] 3.15&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6k60]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6K60 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6K60 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene></td></tr>
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<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=6k60 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6k60 OCA], [http://pdbe.org/6k60 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6k60 RCSB], [http://www.ebi.ac.uk/pdbsum/6k60 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6k60 ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[[http://www.uniprot.org/uniprot/B2MG_HUMAN B2MG_HUMAN]] Defects in B2M are the cause of hypercatabolic hypoproteinemia (HYCATHYP) [MIM:[http://omim.org/entry/241600 241600]]. Affected individuals show marked reduction in serum concentrations of immunoglobulin and albumin, probably due to rapid degradation.<ref>PMID:16549777</ref> Note=Beta-2-microglobulin may adopt the fibrillar configuration of amyloid in certain pathologic states. The capacity to assemble into amyloid fibrils is concentration dependent. Persistently high beta(2)-microglobulin serum levels lead to amyloidosis in patients on long-term hemodialysis.<ref>PMID:3532124</ref> <ref>PMID:1336137</ref> <ref>PMID:7554280</ref> <ref>PMID:4586824</ref> <ref>PMID:8084451</ref> <ref>PMID:12119416</ref> <ref>PMID:12796775</ref> <ref>PMID:16901902</ref> <ref>PMID:16491088</ref> <ref>PMID:17646174</ref> <ref>PMID:18835253</ref> <ref>PMID:18395224</ref> <ref>PMID:19284997</ref>
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== Function ==
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[[http://www.uniprot.org/uniprot/HLAG_HUMAN HLAG_HUMAN]] Involved in the presentation of foreign antigens to the immune system. Plays a role in maternal tolerance of the fetus by mediating protection from the deleterious effects of natural killer cells, cytotoxic T-lymphocytes, macrophages and mononuclear cells. [[http://www.uniprot.org/uniprot/B2MG_HUMAN B2MG_HUMAN]] Component of the class I major histocompatibility complex (MHC). Involved in the presentation of peptide antigens to the immune system.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Human leukocyte Ig-like receptors (LILR) LILRB1 and LILRB2 are immune checkpoint receptors that regulate a wide range of physiological responses by binding to diverse ligands, including HLA-G. HLA-G is exclusively expressed in the placenta, some immunoregulatory cells, and tumors and has several unique isoforms. However, the recognition of HLA-G isoforms by LILRs is poorly understood. In this study, we characterized LILR binding to the beta2-microglobulin (beta2m)-free HLA-G1 isoform, which is synthesized by placental trophoblast cells and tends to dimerize and multimerize. The multimerized beta2m-free HLA-G1 dimer lacked detectable affinity for LILRB1, but bound strongly to LILRB2. We also determined the crystal structure of the LILRB1 and HLA-G1 complex, which adopted the typical structure of a classical HLA class I complex. LILRB1 exhibits flexible binding modes with the alpha3 domain, but maintains tight contacts with beta2m, thus accounting for beta2m-dependent binding. Notably, both LILRB1 and B2 are oriented at suitable angles to permit efficient signaling upon complex formation with HLA-G1 dimers. These structural and functional features of ligand recognition by LILRs provide novel insights into their important roles in the biological regulations.
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Authors:
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Structural and Functional Basis for LILRB Immune Checkpoint Receptor Recognition of HLA-G Isoforms.,Kuroki K, Matsubara H, Kanda R, Miyashita N, Shiroishi M, Fukunaga Y, Kamishikiryo J, Fukunaga A, Fukuhara H, Hirose K, Hunt JS, Sugita Y, Kita S, Ose T, Maenaka K J Immunol. 2019 Nov 6. pii: jimmunol.1900562. doi: 10.4049/jimmunol.1900562. PMID:31694909<ref>PMID:31694909</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 6k60" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Fukunaga, A]]
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[[Category: Fukunaga, Y]]
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[[Category: Hirose, K]]
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[[Category: Kamishikiryo, J]]
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[[Category: Kanda, R]]
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[[Category: Kita, S]]
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[[Category: Kuroki, K]]
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[[Category: Maenaka, K]]
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[[Category: Matsubara, H]]
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[[Category: Miyashita, N]]
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[[Category: Ose, T]]
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[[Category: Shiroishi, M]]
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[[Category: Sugita, Y]]
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[[Category: Hla class i]]
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[[Category: Hlag]]
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[[Category: Immune system]]
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[[Category: Lilrb1/ilt2]]

Revision as of 06:47, 27 November 2019

Structural and functional basis for HLA-G isoform recognition of immune checkpoint receptor LILRBs

PDB ID 6k60

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