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RESEARCH PRODUCT
Histidine tracts in human transcription factors: insight into metal ion coordination ability
Joanna WątłyHenryk KozłowskiJolanta ŚWiatek-kozłowskaMagdalena Rowinska-zyrekAleksandra Hecelsubject
0301 basic medicineinorganic chemicalsMaf Transcription Factors LargeStereochemistryMetal ions in aqueous solutionPeptideNerve Tissue Proteins010402 general chemistry01 natural sciencesBiochemistryInorganic ChemistryMetal03 medical and health scienceschemistry.chemical_compoundCoordination ComplexesAmideImidazoleHomeostasisHumansHistidineAmino Acid SequenceTranscription factorHistidineLigand bindingchemistry.chemical_classificationOriginal PaperMass spectrometryForkhead Transcription FactorsHydrogen-Ion ConcentrationPeptide Fragments0104 chemical sciencesZinc030104 developmental biologyBinding affinitychemistryvisual_artPeptidevisual_art.visual_art_mediumThermodynamicsHuman genomeCopperProtein Bindingdescription
Consecutive histidine repeats are chosen both by nature and by molecular biologists due to their high affinity towards metal ions. Screening of the human genome showed that transcription factors are extremely rich in His tracts. In this work, we examine two of such His-rich regions from forkhead box and MAFA proteins—MB3 (contains 18 His) and MB6 (with 21 His residues), focusing on the affinity and binding modes of Cu2+ and Zn2+ towards the two His-rich regions. In the case of Zn2+ species, the availability of imidazole nitrogen donors enhances metal complex stability. Interestingly, an opposite tendency is observed for Cu2+ complexes at above physiological pH, in which amide nitrogens participate in binding. Electronic supplementary material The online version of this article (10.1007/s00775-017-1512-x) contains supplementary material, which is available to authorized users.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2017-12-01 | Journal of Biological Inorganic Chemistry |