Crystallization and preliminary X-ray diffraction studies of recombinant rabbit interferon-gamma

Samudzi, Cleopas T.; Gribskov, Cynthia L.; Burton, Louis E.; Rubin, John R.

doi:10.1016/0006-291x(91)90155-z

Cited by 3 publications

(1 citation statement)

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“…For other cytokines, it has been shown that their oligomeric state in solution and in the crystal are identical. For example, TNF‐α and interferon‐γ form a trimer and dimer, respectively [39–41], regardless of the method applied. Furthermore, the oligomeric state relates directly to the mode of activation of the receptor of these cytokines.…”

Section: Resultsmentioning

confidence: 99%

Cross‐linking and mutational analysis of the oligomerization state of the cytokine macrophage migration inhibitory factor (MIF)

et al. 1998

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The structure of the cytokine MIF has been investigated by X-ray crystallography, NMR, and biochemical methods with conflicting results regarding the structural and functional oligomerization state of this protein. Determination of the oligomeric state(s) is important for understanding more precisely the molecular mechanism of MIF action. To address this issue, we performed cross-linking of human and mouse MIF and selected mutants by various methods and analyzed the oligomerization by SDS-PAGE and gel filtration. MIF was found to form a mixture of monomeric, dimeric, and trimeric states at physiological concentrations, with the monomer and dimer representing the major species. Similar results were obtained when the carboxy-truncated mutants MIF(1^104) and MIF(1^109) were examined, indicating that the C-terminus of MIF is not critical for trimer stabilization. Cross-linking analysis of the isosteric CysCSer mutants C56S and C80S of human MIF resulted in a similar oligomer distribution, whereas substitution of Cys SW led to a significant reduction in the dimeric and trimeric forms, indicating that the hydrophobic region around Cys SW is important for the oligomerization of MIF. Together, our data argue that physiological MIF solutions contain a mixture of monomers, dimers, and trimers.z 1998 Federation of European Biochemical Societies.

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Section: Resultsmentioning

confidence: 99%