Structural features of the human salivary mucin, MUC7
作者： Tarikere L Gururaja , Narayanan Ramasubbu , Paloth Venugopalan , Molakala S Reddy , Kalaiyarasi Ramalingam
关键词: Glycopeptide 、 Proline 、 Biochemistry 、 Peptide sequence 、 MUC1 、 Stereochemistry 、 Salivary mucin 、 Chemistry 、 Prediction algorithms 、 Polyproline helix 、 Tandem repeat
摘要: Human salivary mucin (MUC7) is characterized by a single polypeptide chain of 357 aa. Detailed analysis the derived MUC7 peptide sequence reveals five distinct regions or domains: (1) an N-terminal basic, histatin-like domain which has leucine-zipper segment, (2) moderately glycosylated domain, (3) six heavily tandem repeats each consisting 23 aa, (4) another MUC1- and MUC2-like (5) C-terminal segment. Chemical semi-empirical prediction algorithms for O-glycosylation suggested that 86/105 (83%) Ser/Thr residues were O-glycosylated with majority located in repeats. The high (∼25%) proline content including 19 diproline segments presence polyproline type structures. CD studies natural synthetic diproline-rich peptides glycopeptides indicated structures do play significant role conformational dynamics MUC7. In addition, crystal structure segment (Boc-Ala-Pro-OBzl) revealed II extended structure. Collectively, data indicate structure, dispersed throughout repeats, may impart stiffening backbone could act consort to keep semi-rigid, rod shaped conformation resembling ‘bottle-brush’ model.
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