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Structural Prediction of the Carbon Terminal End of Human Intestinal Mucin (MUC2) Using Molecular Modeling

V.D. Sadasivan, D.E. Budil, A. Sacco Jr and R.L. Carrier
Northeastern University, US

Keywords:
mucin glycoprotein, MUC2, cysteine-knot

Abstract:
Secretory mucins are the principal determinants of the viscoelastic properties of intestinal mucus, the major barrier to absorption of many drugs. Although mucin is known to play a significant role in inhibition of drug transport and in diseases such as Cystic Fibrosis, its structure remains mostly unknown. A cysteine-rich region (92 residues) exists within the mucin C-terminal domain and is involved in dimer formation. Taking advantage of complete genome sequences in diverse organisms, the present study was undertaken to determine a detailed structure of the C-terminal end of human intestinal mucin (MUC2) via homology modeling. Based on sequence-structure alignments and three-dimensional modeling, a cysteine-knot tertiary structure homologous to that of human chorionic gonadotropin is predicted. The model displays a highly conserved cysteine-knot characteristic, thus providing strong evidence for the existence of the cysteine-knot and novel insight into mucin structure. A comparative experimental study is carried out to validate the model

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