2022
A Cysteine Variant at an Allosteric Site Alters MIF Dynamics and Biological Function in Homo- and Heterotrimeric Assemblies
Skeens E, Pantouris G, Shah D, Manjula R, Ombrello MJ, Maluf NK, Bhandari V, Lisi GP, Lolis EJ. A Cysteine Variant at an Allosteric Site Alters MIF Dynamics and Biological Function in Homo- and Heterotrimeric Assemblies. Frontiers In Molecular Biosciences 2022, 9: 783669. PMID: 35252348, PMCID: PMC8893199, DOI: 10.3389/fmolb.2022.783669.Peer-Reviewed Original ResearchAllosteric siteNon-overlapping functionsEnzymatic activityHeterotrimeric assemblyBiological functionsWild typeCatalytic baseCysteine variantsFunctional interactionHuman macrophage migration inhibitory factorSolvent channelsMacrophage migration inhibitory factorEnzymatic cavityCrystallographic structureNMR dynamicsMixed wild typeVariantsY99CInhibitory factorMammalsNucleaseSubunitsCytosolDifferent extentsFish
1998
Direct link between cytokine activity and a catalytic site for macrophage migration inhibitory factor
Swope M, Sun H, Blake P, Lolis E. Direct link between cytokine activity and a catalytic site for macrophage migration inhibitory factor. The EMBO Journal 1998, 17: 3534-3541. PMID: 9649424, PMCID: PMC1170690, DOI: 10.1093/emboj/17.13.3534.Peer-Reviewed Original ResearchConceptsN-terminal prolineN-terminal regionStructure-based inhibitorsMultiple sequence alignmentThree-dimensional structureInvariant residuesEntire polypeptideMicrobial enzymesCatalytic basePro-1Sequence alignmentMIF homologuesCytokine activityHuman macrophage migration inhibitory factorCatalytic siteProlineInhibitory factorHomologuesUnderlying biological activityP-hydroxyphenylpyruvateProteinMacrophage migration inhibitory factorActive siteBiological activity