 |
PDBsum entry 4wco
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Immune system
|
PDB id
|
|
|
|
4wco
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Crystal structure of extracellular domain of human lectin-Like transcript 1 (llt1), The ligand for natural killer receptor-P1a.
|
|
|
Authors
|
|
S.Kita,
H.Matsubara,
Y.Kasai,
T.Tamaoki,
Y.Okabe,
H.Fukuhara,
J.Kamishikiryo,
E.Krayukhina,
S.Uchiyama,
T.Ose,
K.Kuroki,
K.Maenaka.
|
|
|
Ref.
|
|
Eur J Immunol, 2015,
45,
1605-1613.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
Emerging evidence has revealed the pivotal roles of C-type lectin-like receptors
(CTLRs) in the regulation of a wide range of immune responses. Human natural
killer cell receptor-P1A (NKRP1A) is one of the CTLRs and recognizes another
CTLR, lectin-like transcript 1 (LLT1) on target cells to control NK, NKT and
Th17 cells. The structural basis for the NKRP1A-LLT1 interaction was limitedly
understood. Here, we report the crystal structure of the ectodomain of LLT1. The
plausible receptor-binding face of the C-type lectin-like domain is flat, and
forms an extended β-sheet. The residues of this face are relatively conserved
with another CTLR, keratinocyte-associated C-type lectin, which binds to the
CTLR member, NKp65. A LLT1-NKRP1A complex model, prepared using the crystal
structures of LLT1 and the keratinocyte-associated C-type lectin-NKp65 complex,
reasonably satisfies the charge consistency and the conformational
complementarity to explain a previous mutagenesis study. Furthermore, crystal
packing and analytical ultracentrifugation revealed dimer formation, which
supports a complex model. Our results provide structural insights for
understanding the binding modes and signal transduction mechanisms, which are
likely to be conserved in the CTLR family, and for further rational drug design
towards regulating the LLT1 function.
|
|
|
|
|
|
|
