Crystal structure of extracellular domain of human lectin-like transcript 1 (LLT1), the ligand for natural killer receptor-P1A

Kita, Shunsuke; Matsubara, Haruki; Kasai, Yoshiyuki; Tamaoki, Takaharu; Okabe, Yuki; Fukuhara, Hideo; Kamishikiryo, Jun; Krayukhina, Elena; Uchiyama, Susumu; Ose, Toyoyuki; Kuroki, Kimiko; Maenaka, Katsumi

Crystal structure of extracellular domain of human lectin-like transcript 1 (LLT1), the ligand for natural killer receptor-P1A

Kita, Shunsuke; Matsubara, Haruki; Kasai, Yoshiyuki et al.

European journal of immunology, 2015, 45(6), 1605-1613

Permalink : https://hdl.handle.net/2115/61994

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アクセス権	open access
URI	https://hdl.handle.net/2115/61994
タイトル	Crystal structure of extracellular domain of human lectin-like transcript 1 (LLT1), the ligand for natural killer receptor-P1A
著者	Kita, Shunsuke ; Matsubara, Haruki ; Kasai, Yoshiyuki ; Tamaoki, Takaharu ; Okabe, Yuki ; Fukuhara, Hideo ; Kamishikiryo, Jun ; Krayukhina, Elena ; Uchiyama, Susumu ; Ose, Toyoyuki ; Kuroki, Kimiko ; Maenaka, Katsumi
著者名 Kita, Shunsuke
著者名 Matsubara, Haruki
著者名 Kasai, Yoshiyuki
著者名 Tamaoki, Takaharu
著者名 Okabe, Yuki
著者名 Fukuhara, Hideo
著者名 Kamishikiryo, Jun
著者名 Krayukhina, Elena
e-Rad_Researcher 90335381 著者名 Uchiyama, Susumu
e-Rad_Researcher 80380525 著者名 Ose, Toyoyuki
e-Rad_Researcher 90553313 著者名 Kuroki, Kimiko
e-Rad_Researcher 10322752 著者名 Maenaka, Katsumi
言語	英語
キーワード	Cell surface receptor
	Crystal structure
	C-type lectin-like receptor
	Natural killer cell
	Protein-protein interactions
発行日	2015-06
出版者	Wiley-Blackwell
収録物名	European journal of immunology
巻(号)	45(6)
ページ	1605-1613
抄録	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 -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.
資源タイプ	学術雑誌論文
出版タイプ	Accepted Manuscript
権利情報	This is the peer reviewed version of the following article: Kita, S., Matsubara, H., Kasai, Y., Tamaoki, T., Okabe, Y., Fukuhara, H., Kamishikiryo, J., Krayukhina, E., Uchiyama, S., Ose, T., Kuroki, K. and Maenaka, K. (2015), Crystal structure of extracellular domain of human lectin-like transcript 1 (LLT1), the ligand for natural killer receptor-P1A. Eur. J. Immunol., which has been published in final form at http://dx.doi.org/10.1002/eji.201545509. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Self-Archiving.
PISSN	0014-2980
関連情報	PMID 25826155
関連情報 (isVersionOf)	出版社版DOI https://doi.org/10.1002/eji.201545509