For the record: Chemical modification of a variant of human MIP‐1α; implications for dimer structure

Open Access
Publisher Website
Google Scholar
Abstract
A sequence variant of human MIP‐1α, in which Asp26 has been replaced by Ala, has been chemically modified by the addition of 13C‐labeled methyl groups at each of the lysine residues and the N‐terminus.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‐1α 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‐1β and RANTES.