yeast
Gaetano T. Montelione Laboratory
CABM Protein NMR Laboratory

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Eglin C

Eglin c is a small monomeric protein that belongs to the potato chymotrypsin inhibitor i family of serine protease inhibitors. The proteins that belong to this family are usually small (60-90 amino acid residues in length) and contain no disulfide bonds. Eglin c however, is highly resistant to denaturation by acidification or heat regardless of the lack of disulfide bonds to help stabilize its tertiary structure. Functionally, eglin c is a granulocytic inhibitor of two proteinases: elastase and cathepsin g. The protein occurs naturally in the leech Hirudo medicinalis.
Eglin c is a 70 amino acid residue polypeptide. The protein is colored by secondary structure here: Alpha helix=green, beta sheets=magenta.
  • Keywords: Serine Protease Inhibitor
  • View this protein's PDB entry as 1EGL
  • View this protein's SwissProt entry as ICIC_HIRME

References:

S.G. Hyberts, M.S. Goldberg, T. F. Havel, G. Wagner
The Solution Structure of Eglin C Based on Measurements of Many NOES and Coupling Constants and its Comparison With X-ray Structures.
Protein Science 1:736 (1992)
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