Botos, I., Mori, T., Cartner, L.K., Boyd, M.R., and Wlodawer, A.: Biochem. Biophys. Res. Commun. 294: 184-190, 2002.
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.
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