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STRUCTURAL BIOLOGY: Adaptation of SARS Coronavirus to Humans
Kathryn V. Holmes
In her Perspective, Holmes discusses the elucidation of a crystal structure reported by Li et al. (in the same issue) of the receptor-binding domain of the SARS coronavirus spike glycoprotein bound to its human receptor, angiotensin-converting enzyme 2 (ACE2). The structure reveals how only a few of the many contacting amino acids in the large interface between the spike protein and receptor are critical determinants of the host range of coronavirus binding and entry.
The author is at the University of Colorado Health Sciences Center, Mail Stop 8333, Post Office Box 6211, Aurora, CO 80045, USA. E-mail: kathryn.holmes{at}uchsc.edu
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24, 1627-1638
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MMDB: annotating protein sequences with Entrez's 3D-structure database.
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Highly Conserved Regions within the Spike Proteins of Human Coronaviruses 229E and NL63 Determine Recognition of Their Respective Cellular Receptors..
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J. Virol.
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Human Neutralizing Fab Molecules against Severe Acute Respiratory Syndrome Coronavirus Generated by Phage Display..
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Clin. Vaccine Immunol.
13, 953-957
|Abstract »|Full Text »|PDF »
Defining the Cellular Target(s) of Porcine Reproductive and Respiratory Syndrome Virus Blocking Monoclonal Antibody 7G10.
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80, 689-696
|Abstract »|Full Text »|PDF »
