Four crystal structures of human LLT1, a ligand of human NKR-P1, in varied glycosylation and oligomerization states
- Academy of Sciences of the Czech Republic, v.v.i., Vídeňská 1083, 142 20 Praha 4 (Czech Republic)
- Charles University Prague, Hlavova 8, 128 40 Praha (Czech Republic)
- University of Oxford, Roosevelt Drive, Oxford OX3 7BN (United Kingdom)
- Academy of Sciences of the Czech Republic, v.v.i., Heyrovského nám. 2, 162 06 Praha 6 (Czech Republic)
Four crystal structures of human LLT1, a ligand of human NKR-P1, are reported. 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 GlcNAc{sub 2}Man{sub 5} 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.
- OSTI ID:
- 22347723
- Journal Information:
- Acta Crystallographica. Section D: Biological Crystallography, Vol. 71, Issue Pt 3; Other Information: PMCID: PMC4356368; PMID: 25760607; PUBLISHER-ID: rr5085; OAI: oai:pubmedcentral.nih.gov:4356368; Copyright (c) Skálová et al. 2015; This is an open-access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.; Country of input: International Atomic Energy Agency (IAEA); ISSN 0907-4449
- Country of Publication:
- Denmark
- Language:
- English
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