SEQUENCE DIFFERENCES BETWEEN GLYCOSYLATED AND NONGLYCOSYLATED ASN-X-THR SER ACCEPTOR SITES - IMPLICATIONS FOR PROTEIN ENGINEERING

被引:663
作者
GAVEL, Y [1 ]
VONHEIJNE, G [1 ]
机构
[1] KAROLINSKA INST,NOVUM,CTR BIOTECHNOL,DEPT MOLEC BIOL,S-14152 HUDDINGE,SWEDEN
来源
PROTEIN ENGINEERING | 1990年 / 3卷 / 05期
关键词
Glycoproteins; N-glycosylation; Statistical study;
D O I
10.1093/protein/3.5.433
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
In N-glycosylated glycoproteins, carbohydrate is attached to Asn in the sequence Asn-X-Ser/Thr, where X denotes any amino acid. However, the presence of this consensus peptide does not always lead to glycosylation. We have compiled an extensive collection of glycosylated and non-glycosylated Asn-X-Thr/Ser sites and present a statistical study based on this data set. Our results indicate that non-glycosylated sites tend to be found more frequently towards the C termini of glycoproteins, and that proline residues in positions X and Y in the consensus Asn-X-Thr/Ser-Y strongly reduce the likelihood of N-linked glycosylation. Beyond this, there are no obvious local sequence features that seem to correlate with the absence or presence of N-linked glycosylation. These findings are discussed in terms of the prediction and engineering of glycosylation sites in secretory proteins. © 1990 Oxford University Press.
引用
收藏
页码:433 / 442
页数:10
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