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. 2010 Aug 10;285(43):33230–33241. doi: 10.1074/jbc.M110.120014

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© 2010 by The American Society for Biochemistry and Molecular Biology, Inc.

This article is made available via the PMC Open Access Subset for unrestricted re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for the duration of the COVID-19 pandemic or until permissions are revoked in writing. Upon expiration of these permissions, PMC is granted a perpetual license to make this article available via PMC and Europe PMC, consistent with existing copyright protections.

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FIGURE 2. — nsp10 protein conservation among coronavirus groups 1, 2, and 3. A, sequence alignment of nsp10 proteins derived from genome sequences of the following: SARS-CoV, SARS coronavirus (group 2b, NC_004718), HCoV-OC43, human coronavirus OC43 (group 2a, NC_005147), HCoV-NL63, human coronavirus NL63 (group 1, NC_005831), HCoV-HKU1, human coronavirus HKU1 (group 2a, NC_006577), HCoV-229E, human coronavirus 229E (group 1, NC_002645), IBV, infectious bronchitis virus (group 3a, NC_001451), MHV, mouse hepatitis virus (group 2a, NC_006852), TGEV, transmissible gastroenteritis virus (group 1, NC_002306), BCoV, bovine coronavirus (group 2a, NC_003045), ECoV, equine coronavirus (group 2a, NC_010327), and bat coronavirus, bat-CoV-HKU5–1 (group 2c, NC_009020). The black triangle points to residue 96, colored in blue. The sequences were aligned using the ESPript program (46). Stars indicate residues involved in coordinating zinc atoms. Underlined sequences in blue correspond to clusters of mutations obtained by RY2H. B, nsp10 from SARS-CoV (Protein Data Bank code 2FYG) is depicted in a surface representation. From the alignment above, absolutely conserved residues are shown in red, whereas conserved residues and non-conserved residues are shown in pink and white, respectively. The different amino acids identified as being part of nsp10-nsp16 interaction are named, and the potential surface of interaction is delineated in black.