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PDBsum entry 4qkh
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Immune system
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PDB id
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4qkh
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PDB id:
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Immune system
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Title:
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Dimeric form of human llt1, a ligand for nkr-p1
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Structure:
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C-type lectin domain family 2 member d. Chain: a, b. Fragment: extracellular part, unp residues 72-191. Synonym: lectin-like nk cell receptor, lectin-like transcript 1, llt- 1, osteoclast inhibitory lectin. Engineered: yes. Mutation: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: clax, clec2b, clec2d, llt1, ocil. Expressed in: homo sapiens. Expression_system_taxid: 9606. Expression_system_cell_line: hek293s gnti-.
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Resolution:
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1.80Å
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R-factor:
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0.180
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R-free:
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0.250
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Authors:
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T.Skalova,J.Blaha,K.Harlos,J.Duskova,T.Koval,J.Stransky,J.Hasek, O.Vanek,J.Dohnalek
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Key ref:
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T.Skálová
et al.
(2015).
Four crystal structures of human LLT1, a ligand of human NKR-P1, in varied glycosylation and oligomerization states.
Acta Crystallogr D Biol Crystallogr,
71,
578-591.
PubMed id:
DOI:
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Date:
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06-Jun-14
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Release date:
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11-Mar-15
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PROCHECK
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Headers
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References
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Q9UHP7
(CLC2D_HUMAN) -
C-type lectin domain family 2 member D from Homo sapiens
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Seq:
Struc:
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191 a.a.
123 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 3 residue positions (black
crosses)
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DOI no:
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Acta Crystallogr D Biol Crystallogr
71:578-591
(2015)
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PubMed id:
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Four crystal structures of human LLT1, a ligand of human NKR-P1, in varied glycosylation and oligomerization states.
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T.Skálová,
J.Bláha,
K.Harlos,
J.Dušková,
T.Koval',
J.Stránský,
J.Hašek,
O.Vaněk,
J.Dohnálek.
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ABSTRACT
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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.
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