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

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Title: Crystal structure of extracellular domain of human lectin-like transcript 1 (LLT1), the ligand for natural killer receptor-P1A
Authors: Kita, Shunsuke Browse this author
Matsubara, Haruki Browse this author
Kasai, Yoshiyuki Browse this author
Tamaoki, Takaharu Browse this author
Okabe, Yuki Browse this author
Fukuhara, Hideo Browse this author
Kamishikiryo, Jun Browse this author
Krayukhina, Elena Browse this author
Uchiyama, Susumu Browse this author →KAKEN DB
Ose, Toyoyuki Browse this author →KAKEN DB
Kuroki, Kimiko Browse this author →KAKEN DB
Maenaka, Katsumi Browse this author →KAKEN DB
Keywords: Cell surface receptor
Crystal structure
C-type lectin-like receptor
Natural killer cell
Protein-protein interactions
Issue Date: Jun-2015
Publisher: Wiley-Blackwell
Journal Title: European journal of immunology
Volume: 45
Issue: 6
Start Page: 1605
End Page: 1613
Publisher DOI: 10.1002/eji.201545509
PMID: 25826155
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 -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.
Rights: 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.
Type: article (author version)
URI: http://hdl.handle.net/2115/61994
Appears in Collections:薬学研究院 (Faculty of Pharmaceutical Sciences) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 喜多 俊介

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