Two variant surface glycoproteins of Trypanosoma Brucei of different sequence classes have similar 6 Å resolution X-ray structures View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1987-01

AUTHORS

P Metcalf, M Blum, D Freymann, M Turner, D C Wiley

ABSTRACT

Antigenic variation in the African trypanosome is mediated through changes in the composition of the surface coat. By controlling expression of the major surface protein, the variant surface glycoprotein (VSG), from a repertoire of perhaps 1,000 different genes the organisms exhibit a series of antigenically distinct coats and evade the host's immune system. We have determined the 6 A resolution structure of a T. brucei variant surface glycoprotein, ILTat 1.24, using X-ray crystallography. The crystallized protein consists of the N-terminal two-thirds of the intact VSG which has a relative molecular mass (Mr) of 60,000 (60K). The structure, which includes a 90 A long alpha-helical bundle, is strikingly similar to that of the N-terminal fragment of VSG MITat 1.2 (ref. 4). Although most known VSG sequences show little similarity of primary sequence in the N-terminal domain, the similarity between the structure of a Class I (ILTat 1.24) and a Class II (MITat 1.2) VSG antigen suggests that VSGs may share a common tertiary structure. More... »

PAGES

84

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/325084a0

DOI

http://dx.doi.org/10.1038/325084a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1040333133

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/2432433


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