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Titolo:
PREDICTION OF O-GLYCOSYLATION OF MAMMALIAN PROTEINS - SPECIFICITY PATTERNS OF UDP-GALNAC-POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE
Autore:
HANSEN JE; LUND O; ENGELBRECHT J; BOHR H; NIELSEN JO; HANSEN JES; BRUNAK S;
Indirizzi:
TECH UNIV DENMARK,CTR BIOL SEQUENCE ANAL,BLDG 206 DK-2800 LYNGBY DENMARK UNIV COPENHAGEN,HVIDOVRE HOSP,INFECT DIS LAB DK-2650 HVIDOVRE DENMARK TECH UNIV DENMARK,DEPT PHYS DK-2800 LYNGBY DENMARK
Titolo Testata:
Biochemical journal
, volume: 308, anno: 1995,
parte:, 3
pagine: 801 - 813
SICI:
0264-6021(1995)308:<801:POOOMP>2.0.ZU;2-0
Fonte:
ISI
Lingua:
ENG
Soggetto:
AMINO-ACID-SEQUENCE; SECONDARY STRUCTURE PREDICTION; HUMAN CHORIONIC-GONADOTROPIN; HUMAN TRANSFERRIN RECEPTOR; COLONY-STIMULATING FACTOR; HAMSTER OVARY CELLS; HUMAN GLYCOPHORIN-A; LINKED GLYCOSYLATION; HUMAN-PLASMA; ERYTHROCYTE GLYCOPHORIN;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
104
Recensione:
Indirizzi per estratti:
Citazione:
J.E. Hansen et al., "PREDICTION OF O-GLYCOSYLATION OF MAMMALIAN PROTEINS - SPECIFICITY PATTERNS OF UDP-GALNAC-POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE", Biochemical journal, 308, 1995, pp. 801-813

Abstract

The specificity of the enzyme(s) catalysing the covalent link betweenthe hydroxyl side chains of serine or threonine and the sugar moiety N-acetylgalactosamine (GalNAc) is unknown. Pattern recognition by artificial neural networks and weight matrix algorithms was performed to determine the exact position of in vivo O-linked GalNAc-glycosylated serine and threonine residues from the primary sequence exclusively. Theacceptor sequence context for O-glycosylation of serine was found to differ from that of threonine and the two types were therefore treatedseparately. The context of the sites showed a high abundance of proline, serine and threonine extending far beyond the previously reported region covering positions -4 through +4 relative to the glycosylated residue. The O-glycosylation sites were found to cluster and to have a high abundance in the N-terminal part of the protein. The sites were also found to have an increased preference for three different classes of beta-turns. No simple consensus-like rule could be deduced for the complex glycosylation sequence acceptor patterns. The neural networks were trained on the hitherto largest data material consisting of 48 carefully examined mammalian glycoproteins comprising 264 O-glycosylation sites. For detection neural network algorithms were much more reliable than weight matrices. The networks correctly found 60-95% of the O-glycosylated serine/threonine residues and 88-97% of the non-glycosylated residues in two independent test sets of known glycoproteins. A computer server using E-mail for prediction of O-glycosylation sites hasbeen implemented and made publicly available. The Internet address isNetOglyc@cbs.dtu.dk.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 24/11/20 alle ore 14:15:28