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Nature Structural & Molecular Biology 15, 540 - 542 (2008)
doi:10.1038/nsmb0608-540
Evil versus 'eph-ective' use of ephrin-B2
Benhur Lee1, Zeynep Akyol Ataman1 & Lei Jin1
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Benhur Lee, Zeynep Akyol Ataman and Lei Jin are in the Department of Microbiology, Immunology & Molecular Genetics, David Geffen School of Medicine at the University of California, Los Angeles, California 90095-1489, USA.
e-mail: bleebhl@ucla.edu
Abstract
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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Structural basis of Nipah and Hendra virus attachment to their cell-surface receptor ephrin-B2Nature Structural & Molecular Biology Article (01 Jun 2008)
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