Literature DB >> 3814765

Do asparagine-linked carbohydrate chains in glycoproteins have a preference for beta-bends?

J J Beintema.   

Abstract

X-ray structures of the conformation of carbohydrate moieties and connected regions of glycoproteins are summarized. Evidence is presented that there is some preference for carbohydrate attachment at beta-bends. Evolution may have favored glycosylation to occur at bends to ensure free mobility of the carbohydrate moieties.

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Year:  1986        PMID: 3814765     DOI: 10.1007/bf01116537

Source DB:  PubMed          Journal:  Biosci Rep        ISSN: 0144-8463            Impact factor:   3.840


  3 in total

1.  Kinetics of folding and association of differently glycosylated variants of invertase from Saccharomyces cerevisiae.

Authors:  G Kern; D Kern; R Jaenicke; R Seckler
Journal:  Protein Sci       Date:  1993-11       Impact factor: 6.725

2.  Conformational implications of asparagine-linked glycosylation.

Authors:  B Imperiali; K W Rickert
Journal:  Proc Natl Acad Sci U S A       Date:  1995-01-03       Impact factor: 11.205

3.  Effect of Glycosylation on an Immunodominant Region in the V1V2 Variable Domain of the HIV-1 Envelope gp120 Protein.

Authors:  Jianhui Tian; Cesar A López; Cynthia A Derdeyn; Morris S Jones; Abraham Pinter; Bette Korber; S Gnanakaran
Journal:  PLoS Comput Biol       Date:  2016-10-07       Impact factor: 4.475

  3 in total

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