Zinc Finger Collection
Teaching Points View document as PDF
When proteins fold into their tertiary structures, there are often subdivisions within the protein, designated as domains, which are characterized by similar features or motifs. One such motif is the zinc finger, in which a specific domain of the protein is arranged into a "finger-like" structure where two strands beta sheet and one alpha helix are positioned around a zinc ion. The zinc finger motif is commonly found in eukaryotic transcription factors, which are proteins that bind to specific sequences of DNA in order to regulate transcription.
One common class of zinc finger is the C2H2 class which is the one modeled in this collection. In this class of zinc fingers, the zinc ion is bound to two cysteine residues and to two histidine residues. With this collection, students can visualize the folding of the polypeptide chain into the α-helix and β-sheets to produce the "finger-like" structure and to see the interaction of the side chains of histidine and cysteine with the zinc ion. In addition to the backbone models, this collection also includes a model representing the electrostatic potential of the surface of the zinc finger, allowing students to examine the surface of the protein.
Models in this Collection
- Zinc finger α-carbon backbone model
- Zinc finger α-carbon backbone model with Zn attached to histidine and cysteine residues, in wireframe
- Zinc finger α-carbon backbone model with Zn; all amino acid residues in wireframe
- Zinc finger wireframe model without sidechains
- Zinc finger wireframe model without sidechains; Zn attached to histidine and cysteine residues, also displayed in wireframe
- Zinc finger model with all amino acid residues in wireframe; Zn in spacefill
- Zinc finger surface model
Model Details
- Zinc finger α-carbon backbone model
- Based on PDB file 1ZAA
- Residues 4-31 displayed
- Model in white
- Model made of nylon on the SLS machine
- Zinc finger α-carbon backbone model with Zn attached to histidine and cysteine residues, in wireframe
- Based on PDB file 1ZAA
- Residues 4-31 displayed
- Alpha carbon backbone in white
- Amino acid residues in CPK colors
- Zn is displayed in spacefill and is green
- Model made of nylon on the SLS machine
- Zinc finger α-carbon backbone model with Zn; all amino acid residues in wireframe
- Based on PDB file 1ZAA
- Residues 4-31 displayed
- Alpha carbon backbone in white
- Amino acid residues in CPK colors
- Zn is displayed in spacefill and is green
- Model made of nylon on the SLS machine
- Zinc finger wireframe model without sidechains
- Based on PDB file 1ZAA
- Residues 4-31 displayed
- Amino acids in CPK colors
- Zn is displayed in spacefill and is green
- Model made of nylon on the SLS machine
- Zinc finger wireframe model without sidechains; Zn attached to histidine and cysteine residues, also displayed in wireframe
- Based on PDB file 1ZAA
- Residues 4-31 displayed
- Amino acids in CPK colors
- Zn is displayed in spacefill and is green
- Hydrogen bonds on α-helix in white
- Model made of nylon on the SLS machine
- Zinc finger model with all amino acid residues in wireframe; Zn in spacefill
- Based on PDB file 1ZAA
- Residues 4-31 displayed
- Amino acids in CPK colors
- Zn is displayed in spacefill and is green
- Model made of nylon on the SLS machine
- Zinc finger surface model
- Based on PDB file 1ZAA
- Residues 4-31 displayed
- Surface model
- Uncharged regions in white
- Positively charged regions in blue
- Negatively charged regions in red
- Model made of plaster on the ZCorp printer, then coated with lacquer