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Insight into E-selectin/ligand interaction from the crystal structure and mutagenesis of the lec/EGF domains

Nature volume 367, pages 532–538 (1994)Cite this article

Abstract

The three-dimensional structure of the ligand-binding region of human E-selectin has been determined at 2.0 Å resolution. The structure reveals limited contact between the two domains and a coordination of Ca2+ not predicted from other C-type lectins. Structure/function analysis indicates a defined region and specific amino-acid side chains that may be involved in ligand binding. These features of the E-selectin/ligand interaction have important implications for understanding the recruitment of leukocytes to sites of inflammation.

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Author notes

  1. John M. Rumberger & Daniel K. Burns

    Present address: Glaxo Research Institute, Department of Cell Physiology, Research Triangle Park, North Carolina, 27709, USA

Authors and Affiliations

  1. Roche Research Center, Hoffmann-La Roche Inc., Nutley, New Jersey, 07110, USA

    Bradford J. Graves, Robert L. Crowther, Chitra Chandran, John M. Rumberger, Shirley Li, Kuo-Sen Huang, David H. Presky, Philip C. Familletti, Barry A. Wolitzky & Daniel K. Burns

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  1. Bradford J. Graves
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Graves, B., Crowther, R., Chandran, C. et al. Insight into E-selectin/ligand interaction from the crystal structure and mutagenesis of the lec/EGF domains. Nature 367, 532–538 (1994). https://doi.org/10.1038/367532a0

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