Atomic-resolution crystal structure of the antiviral lectin scytovirin |
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Authors: | Moulaei Tinoush Botos Istvan Ziółkowska Natasza E Bokesch Heidi R Krumpe Lauren R McKee Tawnya C O'Keefe Barry R Dauter Zbigniew Wlodawer Alexander |
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Affiliation: | Protein Structure Section, Macromolecular Crystallography Laboratory, National Cancer Institute, NCI-Frederick, Frederick, Maryland 21702-1201, USA. |
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Abstract: | The crystal structures of the natural and recombinant antiviral lectin scytovirin (SVN) were solved by single-wavelength anomalous scattering and refined with data extending to 1.3 A and 1.0 A resolution, respectively. A molecule of SVN consists of a single chain 95 amino acids long, with an almost perfect sequence repeat that creates two very similar domains (RMS deviation 0.25 A for 40 pairs of Calpha atoms). The crystal structure differs significantly from a previously published NMR structure of the same protein, with the RMS deviations calculated separately for the N- and C-terminal domains of 5.3 A and 3.7 A, respectively, and a very different relationship between the two domains. In addition, the disulfide bonding pattern of the crystal structures differs from that described in the previously published mass spectrometry and NMR studies. |
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Keywords: | lectins new fold anomalous scattering scytovirin |
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