The Journal of Experimental Medicine
BioLegend: New Th17, Treg Tools
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents
Published online 8 January 2001.
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Citation Map
Services
Right arrow Email this article
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new content in the JEM
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Matsumoto, N.
Right arrow Articles by Yamamoto, K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Matsumoto, N.
Right arrow Articles by Yamamoto, K.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?
© The Rockefeller University Press, 0022-1007/2001/1/147/ $5.00
The Journal of Experimental Medicine, Volume 193, Number 2, January 15, 2001 147-158

Original Article

The Functional Binding Site for the C-type Lectin–like Natural Killer Cell Receptor Ly49A Spans Three Domains of Its Major Histocompatibility Complex Class I Ligand

Naoki Matsumotoa, Motoaki Mitsukia, Kyoko Tajimaa, Wayne M. Yokoyamab, and Kazuo Yamamotoa
a Laboratory of Molecular Medicine, Department of Integrated Biosciences, The University of Tokyo Graduate School of Frontier Sciences, Tokyo 113-0033, Japan
b Howard Hughes Medical Institute, Washington University School of Medicine, St. Louis, Missouri 63110

Correspondence to: Naoki Matsumoto, Laboratory of Molecular Medicine, Department of Integrated Biosciences, The University of Tokyo Graduate School of Frontier Sciences, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan. Tel:81-3-5841-8785 Fax:81-3-5841-8923 E-mail:nmatsu{at}k.u-tokyo.ac.jp.

Natural killer (NK) cells express receptors that recognize major histocompatibility complex (MHC) class I molecules and regulate cytotoxicity of target cells. In this study, we demonstrate that Ly49A, a prototypical C-type lectin–like receptor expressed on mouse NK cells, requires species-specific determinants on ß2-microglobulin (ß2m) to recognize its mouse MHC class I ligand, H-2Dd. The involvement of ß2m in the interaction between Ly49A and H-2Dd is also demonstrated by the functional effects of a ß2m-specific antibody. We also define three residues in {alpha}1/{alpha}2 and {alpha}3 domains of H-2Dd that are critical for the recognition of H-2Dd on target cells by Ly49A. In the crystal structure of the Ly49A/H-2Dd complex, these residues are involved in hydrogen bonding to Ly49A in one of the two potential Ly49A binding sites on H-2Dd. These data unambiguously indicate that the functional effect of Ly49A as an MHC class I–specific NK cell receptor is mediated by binding to a concave region formed by three structural domains of H-2Dd, which partially overlaps the CD8 binding site.

Key Words: ß2-microglobulin, inhibitory receptor, cytotoxicity, mutation, H-2 antigens


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:



  Home | Help | Feedback | Subscriptions | Archive | Search
TABLE OF CONTENTS