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

Autor: Ji-Chun Yang, Lloyd George Czaplewski, P. G. Varley, J. Fisher, P. Tan, J. T. Ashfield, T. Meyers, J. R. P. Arnold, D. Lowne, T. Dudgeon
Rok vydání: 2000
Předmět:
Zdroj: Protein Science. 9:2047-2053
ISSN: 1469-896X
0961-8368
DOI: 10.1110/ps.9.10.2047
Popis: A sequence variant of human MIP-1alpha, in which Asp26 has been replaced by Al alpha, has been chemically modified by the addition of 13C-labeled methyl groups at each of the lysine residues and the N-terminus.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.
Databáze: OpenAIRE