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| | ==Dimeric form of human LLT1, a ligand for NKR-P1== | | ==Dimeric form of human LLT1, a ligand for NKR-P1== |
| - | <StructureSection load='4qkh' size='340' side='right' caption='[[4qkh]], [[Resolution|resolution]] 1.80Å' scene=''> | + | <StructureSection load='4qkh' size='340' side='right'caption='[[4qkh]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4qkh]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QKH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QKH FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4qkh]] is a 2 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=4QKH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QKH FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4qkg|4qkg]], [[4qki|4qki]], [[4qkj|4qkj]]</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=4qkh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qkh OCA], [https://pdbe.org/4qkh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qkh RCSB], [https://www.ebi.ac.uk/pdbsum/4qkh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qkh ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CLAX, CLEC2B, CLEC2D, LLT1, OCIL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4qkh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qkh OCA], [http://pdbe.org/4qkh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4qkh RCSB], [http://www.ebi.ac.uk/pdbsum/4qkh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4qkh ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CLC2D_HUMAN CLC2D_HUMAN]] Receptor for KLRB1 that protects target cells against natural killer cell-mediated lysis. Inhibits osteoclast formation. Inhibits bone resorption. Modulates the release of interferon-gamma. Binds high molecular weight sulfated glycosaminoglycans.<ref>PMID:14753741</ref> <ref>PMID:15104121</ref> <ref>PMID:16339513</ref> | + | [https://www.uniprot.org/uniprot/CLC2D_HUMAN CLC2D_HUMAN] Receptor for KLRB1 that protects target cells against natural killer cell-mediated lysis. Inhibits osteoclast formation. Inhibits bone resorption. Modulates the release of interferon-gamma. Binds high molecular weight sulfated glycosaminoglycans.<ref>PMID:14753741</ref> <ref>PMID:15104121</ref> <ref>PMID:16339513</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Blaha, J]] | + | [[Category: Large Structures]] |
| - | [[Category: Dohnalek, J]] | + | [[Category: Blaha J]] |
| - | [[Category: Duskova, J]] | + | [[Category: Dohnalek J]] |
| - | [[Category: Harlos, K]] | + | [[Category: Duskova J]] |
| - | [[Category: Hasek, J]] | + | [[Category: Harlos K]] |
| - | [[Category: Koval, T]] | + | [[Category: Hasek J]] |
| - | [[Category: Skalova, T]] | + | [[Category: Koval T]] |
| - | [[Category: Stransky, J]] | + | [[Category: Skalova T]] |
| - | [[Category: Vanek, O]] | + | [[Category: Stransky J]] |
| - | [[Category: Anchored in membrane on cell surface]]
| + | [[Category: Vanek O]] |
| - | [[Category: C-type lectin like fold]]
| + | |
| - | [[Category: Deglycosylated after the first glcnac unit]]
| + | |
| - | [[Category: Glycosylation]]
| + | |
| - | [[Category: Immune system]]
| + | |
| - | [[Category: Ligand for human receptor nkr-p1]]
| + | |
| Structural highlights
Function
CLC2D_HUMAN Receptor for KLRB1 that protects target cells against natural killer cell-mediated lysis. Inhibits osteoclast formation. Inhibits bone resorption. Modulates the release of interferon-gamma. Binds high molecular weight sulfated glycosaminoglycans.[1] [2] [3]
Publication Abstract from PubMed
Human LLT1 is a C-type lectin-like ligand of NKR-P1 (CD161, gene KLRB1), a C-type lectin-like receptor of natural killer cells. Using X-ray diffraction, the first experimental structures of human LLT1 were determined. Four structures of LLT1 under various conditions were determined: monomeric, dimeric deglycosylated after the first N-acetylglucosamine unit in two forms and hexameric with homogeneous GlcNAc2Man5 glycosylation. The dimeric form follows the classical dimerization mode of human CD69. The monomeric form keeps the same fold with the exception of the position of an outer part of the long loop region. The hexamer of glycosylated LLT1 consists of three classical dimers. The hexameric packing may indicate a possible mode of interaction of C-type lectin-like proteins in the glycosylated form.
Four crystal structures of human LLT1, a ligand of human NKR-P1, in varied glycosylation and oligomerization states.,Skalova T, Blaha J, Harlos K, Duskova J, Koval' T, Stransky J, Hasek J, Vanek O, Dohnalek J Acta Crystallogr D Biol Crystallogr. 2015 Mar;71(Pt 3):578-91. doi:, 10.1107/S1399004714027928. Epub 2015 Feb 26. PMID:25760607[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hu YS, Zhou H, Myers D, Quinn JM, Atkins GJ, Ly C, Gange C, Kartsogiannis V, Elliott J, Kostakis P, Zannettino AC, Cromer B, McKinstry WJ, Findlay DM, Gillespie MT, Ng KW. Isolation of a human homolog of osteoclast inhibitory lectin that inhibits the formation and function of osteoclasts. J Bone Miner Res. 2004 Jan;19(1):89-99. PMID:14753741 doi:http://dx.doi.org/10.1359/JBMR.0301215
- ↑ Mathew PA, Chuang SS, Vaidya SV, Kumaresan PR, Boles KS, Pham HT. The LLT1 receptor induces IFN-gamma production by human natural killer cells. Mol Immunol. 2004 Mar;40(16):1157-63. PMID:15104121
- ↑ Rosen DB, Bettadapura J, Alsharifi M, Mathew PA, Warren HS, Lanier LL. Cutting edge: lectin-like transcript-1 is a ligand for the inhibitory human NKR-P1A receptor. J Immunol. 2005 Dec 15;175(12):7796-9. PMID:16339513
- ↑ Skalova T, Blaha J, Harlos K, Duskova J, Koval' T, Stransky J, Hasek J, Vanek O, Dohnalek J. Four crystal structures of human LLT1, a ligand of human NKR-P1, in varied glycosylation and oligomerization states. Acta Crystallogr D Biol Crystallogr. 2015 Mar;71(Pt 3):578-91. doi:, 10.1107/S1399004714027928. Epub 2015 Feb 26. PMID:25760607 doi:http://dx.doi.org/10.1107/S1399004714027928
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