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Domain-swapped structure of a mutant of cyanovirin-N

  1. Author:
    Botos, I.
    Mori, T.
    Cartner, L. K.
    Boyd, M. R.
    Wlodawer, A.

  2. Author Address

    NCI, Macromol Crystallog Lab, Frederick, MD 21702 USA NCI, Macromol Crystallog Lab, Frederick, MD 21702 USA NCI, Ctr Canc Res, Mol Targets Drug Discovery Program, Frederick, MD 21702 USA NCI, Sci Applicat Int Corp, Frederick, MD 21702 USA Wlodawer A NCI, Macromol Crystallog Lab, Frederick, MD 21702 USA
    1. Year: 2002
  2. Journal: Biochemical and Biophysical Research Communications
    1. 294
    2. 1
    3. Pages: 184-190
  4. Type of Article: Article
  1. Abstract:

    Cyanovirin-N (CV-N) is a potent 11 kDa HIV-inactivating protein that binds with high affinity to the HIV surface envelope protein gp120. A double mutant P51S/S52P of CV-N was engineered by swapping two critical hinge-region residues Pro51 and Ser52. This mutant has biochemical and biophysical characteristics equivalent to the wild-type CV-N and its structure resembles that of wild-type CV-N. However, the mutant shows a different orientation in the hinge region that connects two domains of the protein. The observation that this double mutant crystallizes under a wide variety of conditions challenges some of the current hypotheses on domain swapping and on the role of hinge-region proline residues in domain orientation. The current structure contributes to the understanding of domain swapping in cyanovirins, permitting rational design of domain- swapped CV-N mutants. (C) 2002 Published by Elsevier Science (USA).

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