by Joel Mackay | Dec 4, 2020 | Structure Gallery |
[ PDB file ] [ PubMed link ] ZNF265 is a mammalian splicing factor, which contains an Arg-Ser rich domain and a putative double zinc finger motif that is capable of binding to RNA (putting it in the SR class of proteins). Shown here is the structure of one of the two...
by Joel Mackay | Oct 20, 2020 | Structure Gallery |
[ PDB file ] [ PubMed link ] This non-native structure corresponds to a fragment of the CH1 domain of CBP. Although the CH1 domain in its native form binds 3 zinc ions (Dames et al, PNAS 2002, 99, 5271-5276), this shorter domain binds only one zinc ion, through a...
by Joel Mackay | Jul 23, 2000 | Structure Gallery |
[ PDB file ] [ PubMed link ] USF9 has the same zinc ligation topology as USF1 but the two fingers share only 14% sequence identity outside of the zinc ligands (blue). However, USF9 adopts an almost identical fold to USF1, with a short β-hairpin (orange) and an...
by Joel Mackay | Jul 23, 2000 | Structure Gallery |
[ PDB file ] [ PubMed link ] U-shaped is a member of the FOG family of transcription factors, which interact with GATA proteins to control gene expression in various tissues. U-shaped has nine zinc fingers. The structure of the first finger of U-shaped (USF1) is very...
by Joel Mackay | Jul 23, 1999 | Structure Gallery |
[ PDB file ] [ PubMed link ] The structure of GNF consists of two distorted β-hairpins and an α-helix, with a central zinc atom (green) ligated by four cysteine residues (red). GATA-1 interacts with transcription factors from the FOG family using this N-terminal zinc...