Ferguson ZNF Sandbox: Difference between revisions
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==The Zinc Finger== | ==The Zinc Finger== | ||
The DNA-binding motif known as the zinc finger was first discovered by Klug in Transcription Factor IIIA in ''Xenopus laevis'', the African clawed toad. TFIIIA is a 344 residue protein that contains 9 repeated modules, which are about 30 residues each, that contain two invariant Cys residues and two invariant His residues. These are able to bind a zinc ion, allowing the protein to fold tightly around it. This protein stabilizer is found in thousands of different proteins in both plants and animals, but not in prokaryotic organisms. | The DNA-binding motif known as the zinc finger was first discovered by Klug in Transcription Factor IIIA in ''Xenopus laevis'', the African clawed toad. TFIIIA is a 344 residue protein that contains 9 repeated modules, which are about 30 residues each, that contain two invariant Cys residues and two invariant His residues<ref>Voet, Donald; Voet, Judith G.; Pratt, Charlotte W. Fundamentals of Biochemistry: Life at the Molecular Level. 3rd Ed. Hoboken, NJ: Wiley, 2008</ref>. These are able to bind a zinc ion, allowing the protein to fold tightly around it. This protein stabilizer is found in thousands of different proteins in both plants and animals, but not in prokaryotic organisms. | ||
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===Zinc Finger Structure=== | ===Zinc Finger Structure=== | ||
The zinc fingers of a protein are normally 20 to 30 amino acids in length and help to create a solid, stable structure <ref> | The zinc fingers of a protein are normally 20 to 30 amino acids in length and help to create a solid, stable structure <ref>Goodsell, David. Zinc Fingers. RCSB. PDB. March, 2007. Web</ref>. | ||
==Reference== | ==Reference== | ||
<references/> | <references/> | ||
