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The structure of MCP-1 in two crystal forms provides a rare example of variable quaternary interactions

Nature Structural Biology volume 4, pages 64–69 (1997)Cite this article

Abstract

The X-ray crystal structure of recombinant human monocyte chemoattractant protein (MCP-1) has been solved in two crystal forms. One crystal form (P), refined to 1.85 Å resolution, contains a dimer in the asymmetric unit, while the other (I) contains a monomer and was refined at 2.4 Å. Although both crystal forms grow together in the same droplet, the respective quaternary structures of the protein differ dramatically. In addition, both X-ray structures differ to a similar extent from the solution structure of MCP-1. Such extent of variability of quaternary structures is unprecedented. In the crystal structures, the well-ordered N termini of MCP-1 form 310-helices. Comparison of the three MCP-1 structures revealed a direct correlation between the main-chain conformation of the first two cysteine residues and the quaternary arrangements. These data can be used to explain the structural basis for the assignment of residues responsible for biological activity.

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Author information

Authors and Affiliations

  1. Macromolecular Structure Laboratory, NCI-Frederick Cancer Research and Development Center, ABL-Basic Research Program, Frederick, Maryland, 21702, USA

    Jacek Lubkowski, Grzegorz Bujacz, Lluís Boqué & Wlodawer Alexander

  2. The DuPont Merck Pharmaceutical Company, Chemical & Physical Sciences, Wilmington, Delaware, 19880, USA

    Domaille Peter J.

  3. Department of Molecular and Cell Biology, University of California at Berkeley, Berkeley, California, 94720, USA

    Handel Tracy M.

  4. Faculty of Food Chemistry and Biotechnology, Technical University of Lódź, 90924, Lódź, Poland

    Grzegorz Bujacz

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Lubkowski, J., Bujacz, G., Boqué, L. et al. The structure of MCP-1 in two crystal forms provides a rare example of variable quaternary interactions. Nat Struct Mol Biol 4, 64–69 (1997). https://doi.org/10.1038/nsb0197-64

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