4qkj
From Proteopedia
Glycosylated form of human LLT1, a ligand for NKR-P1, in this structure forming hexamers
Structural highlights
FunctionCLC2D_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 PubMedHuman 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
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Categories: Homo sapiens | Large Structures | Blaha J | Dohnalek J | Duskova J | Hasek J | Koval T | Skalova T | Stransky J | Vanek O
