A structural motif in the variant surface glycoproteins of Trypanosoma brucei View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1993-04

AUTHORS

M L Blum, J A Down, A M Gurnett, M Carrington, M J Turner, D C Wiley

ABSTRACT

The variable domain of the trypanosome variant surface glycoprotein (VSG) ILTat 1.24 has been shown by X-ray crystallography to resemble closely the structures of VSG MITat 1.2, despite their low sequence similarity. Specific structural features of these VSGs, including substitution of carbohydrate for an alpha-helix, can be found in other VSG sequences. Thus antigenic variation in trypanosomes is accomplished by sequence variation, not gross structural alteration; the extensive sequence differences among VSGs may be required for another reason, such as the avoidance of recognition by helper T cells. Additionally, VSG sequences are found to define families, within a VSG superfamily, which have evolved in the trypanosome genome. More... »

PAGES

603-609

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/362603a0

DOI

http://dx.doi.org/10.1038/362603a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1006471151

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/8464512


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