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. 2010 Feb 10;285(17):13057–13065. doi: 10.1074/jbc.M109.094938

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© 2010 by The American Society for Biochemistry and Molecular Biology, Inc.

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FIGURE 1. — Sequences and schematic representation of CV-N variants. Domains and respective sequences are color-coded, with domain A in green and domain B in pink. Mutated residues are colored in blue. Disulfide bonds are indicated by brackets. A, amino acid sequence of (P51G)CV-N. In this protein the two binding sites are separated by ∼40 Å. B, amino acid sequence of the disulfide-linked monomer (CVN^ΔA)_ssm. The intramolecular disulfide is shown as a yellow bracket. This protein contains only one binding site in domain B. C, amino acid sequence of the disulfide-linked dimer (CVN^ΔA)_ssd. This head-to-head linked dimer contains binding sites in domains B and B′ only, and they are separated by ∼57 Å. D, amino acid sequence of CVN^mutDB. This protein contains only one binding site in domain A. E, amino acid sequence of the domain-swapped dimer (CVN^ΔB)_dsd. This protein contains binding sites on domains A and A′ only, and they are separated by ∼48 Å.