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Protein Science, Vol 9, Issue 10 2047-2053, Copyright © 2000 by The Protein Society

Chemical modification of a variant of human MIP-1alpha; implications for dimer structure [In Process Citation]

JT Ashfield, T Meyers, D Lowne, PG Varley, JR Arnold, P Tan, JC Yang, LG Czaplewski, T Dudgeon and J Fisher
School of Chemistry, University of Leeds, United Kingdom.

A sequence variant of human MIP-1alpha, in which Asp26 has been replaced by Al alpha, has been chemically modified by the addition of 13C-labeled methyl groups at each of the lysine residues and the N- terminus. The sites of methylation have been verified by a combination of MALDI-TOF mass spectrometric experiments and tryptic digestion followed by N-terminal mapping. The effect of the modification on the structure and activity of the protein have been determined by analytical ultra-centrifugation, 13C NMR spectroscopy and receptor binding studies. The results of these experiments suggest that huMIP- alpha D26A (BB10010), when present as a dimer, adopts a globular structure, like MCP-3, rather than the elongated or cylindrical structure determined for dimers of huMIP-1beta and RANTES.
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