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Science 25 March 1994:
Vol. 263. no. 5154, pp. 1762 - 1767
DOI: 10.1126/science.8134838
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Articles

Science, Vol 263, Issue 5154, 1762-1767
Copyright © 1994 by American Association for the Advancement of Science

articles

High-resolution solution structure of the beta chemokine hMIP-1 beta by multidimensional NMR

PJ Lodi, DS Garrett, J Kuszewski, ML Tsang, JA Weatherbee, WJ Leonard, AM Gronenborn, and GM Clore

Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892.

The three-dimensional structure of a member of the beta subfamily of chemokines, human macrophage inflammatory protein-1 beta (hMIP-1 beta), has been determined with the use of solution multidimensional heteronuclear magnetic resonance spectroscopy. Human MIP-1 beta is a symmetric homodimer with a relative molecular mass of approximately 16 kilodaltons. The structure of the hMIP-1 beta monomer is similar to that of the related alpha chemokine interleukin-8 (IL-8). However, the quaternary structures of the two proteins are entirely distinct, and the dimer interface is formed by a completely different set of residues. Whereas the IL-8 dimer is globular, the hMIP-1 beta dimer is elongated and cylindrical. This provides a rational explanation for the absence of cross-binding and reactivity between the alpha and beta chemokine subfamilies. Calculation of the solvation free energies of dimerization suggests that the formation and stabilization of the two different types of dimers arise from the burial of hydrophobic residues.


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