4QKJ

Glycosylated form of human LLT1, a ligand for NKR-P1, in this structure forming hexamers

Summary for 4QKJ

• Entry DOI: 10.2210/pdb4qkj/pdb
• Related: 4QKG 4QKH 4QKI
• Descriptor: C-type lectin domain family 2 member D, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
• Functional Keywords: c-type lectin like fold, ligand for human receptor nkr-p1, glcnac2man5 glycosylation, anchored in membrane on cell surface, immune system
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 15913.57

Authors

Skalova, T.,Blaha, J.,Duskova, J.,Koval, T.,Stransky, J.,Hasek, J.,Vanek, O.,Dohnalek, J. (deposition date: 2014-06-06, release date: 2015-03-11, Last modification date: 2024-11-20)

Primary citation

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.,Sect.D, 71:578-591, 2015

PubMed Abstract: 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.

PubMed: 25760607
DOI: 10.1107/S1399004714027928

Experimental method

X-RAY DIFFRACTION (2.75 Å)