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The domain-swapped dimer of cyanovirin-N is in a metastable folded state: Reconciliation of X-ray and NMR structures

  1. Author:
    Barrientos, L. G.
    Louis, J. M.
    Botos, I.
    Mori, T.
    Han, Z. Z.
    O'Keefe, B. R.
    Boyd, M. R.
    Wlodawer, A.
    Gronenborn, A. M.

  2. Author Address

    NIDDKD, Chem Phys Lab, NIH, Bethesda, MD 20892 USA NIDDKD, Chem Phys Lab, NIH, Bethesda, MD 20892 USA NCI, Macromol Crystallog Lab, Frederick, MD 21702 USA NCI, Ctr Canc Res, Mol Targets Drug Discovery Program, Frederick, MD 21702 USA Gronenborn AM NIDDKD, Chem Phys Lab, NIH, Bethesda, MD 20892 USA
    1. Year: 2002
  2. Journal: Structure
    1. 10
    2. 5
    3. Pages: 673-686
  4. Type of Article: Article
  1. Abstract:

    The structure of the potent HIV-inactivating protein cyanovirin-N was previously found by NMR to be a monomer in solution and a domain-swapped dimer by X-ray crystallography. Here we demonstrate that in solution, CV-N can exist both in monomeric an in domain-swapped dimeric form. The dimer is a metastable, kinetically trapped structure at neutral pH and room temperature. Based on orientational NMR constraints, we show that the domain-swapped solution dimer is similar to structures in two different crystal forms, exhibiting solely a small reorientation around the hinge region. Mutation of the single proline residue in the hinge to glycine significantly stabilizes the protein in both its monomeric and dimeric forms. By contrast, mutation of the neighboring serine to proline results in an exclusively dimeric protein, caused by a drastic destabilization of the monomer.

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