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Evil versus 'eph-ective' use of ephrin-B2

Nature Structural & Molecular Biology volume 15, pages 540–542 (2008)Cite this article

Crystal structures of the Nipah and Hendra virus attachment protein complexed with ephrin-B2 shed light on the apparent paradox of ephrin-B2's flexibility for binding multiple receptors. Surprisingly, the switch from the use of glycan-based to protein-based receptors seems to have evolved independently from other protein-receptor–using paramyxoviruses such as the measles virus.

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Figure 1: Structural phylogeny of six-bladed β-propellers.
Figure 2: EFNB2–binding partner interactions and potential consequences.

Katie Ris-Vicari

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  1. Zeynep Akyol Ataman and Lei Jin are in the Department of Microbiology, Benhur Lee, Immunology & Molecular Genetics, David Geffen School of Medicine at the University of California, Los Angeles, California 90095-1489, USA. bleebhl@ucla.edu,

    Benhur Lee, Zeynep Akyol Ataman & Lei Jin

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  1. Benhur Lee
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  2. Zeynep Akyol Ataman
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Lee, B., Ataman, Z. & Jin, L. Evil versus 'eph-ective' use of ephrin-B2. Nat Struct Mol Biol 15, 540–542 (2008). https://doi.org/10.1038/nsmb0608-540

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