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Atomic-resolution crystal structure of the antiviral lectin scytovirin

  1. Author:
    Moulaei, T.
    Botos, I.
    Ziolkowska, N. E.
    Bokesch, H. R.
    Krumpe, L. R.
    McKee, T. C.
    O'Keefe, B. R.
    Dauter, Z.
    Wlodawer, A.

  2. Author Address

    NCI, Macromol Crystallog Lab, Prot Struct Sect, Ft Detrick, MD 21702 USA. NCI, Ctr Canc Res, Mol Targets Dev Program, Ft Detrick, MD 21702 USA. NCI, SAIC Frederick Inc, Ft Detrick, MD 21702 USA. Argonne Natl Lab, Natl Canc Inst, Macromol Crystallog Lab, Synchrotron Radiat Res Sect, Argonne, IL 60439 USA.;Wlodawer, A, NCI, Macromol Crystallog Lab, Ft Detrick, MD 21702 USA.;wlodawer@ncifcrf.gov
    1. Year: 2007
    2. Date: Dec
  2. Journal: Protein Science
    1. 16
    2. 12
    3. Pages: 2756-2760
  4. Type of Article: Article
  5. ISSN: 0961-8368
  1. 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 angstrom and 1.0 angstrom 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 angstrom for 40 pairs of C alpha 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 angstrom and 3.7 angstrom, 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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External Sources

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  2. DOI: 10.1110/ps.073157507
  3. View record in Web of Science®
  4. WOS: 000251081300021

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