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