2VSG
A Structural Motif in the Variant Surface Glycoproteins of Trypanosoma Brucei
Summary for 2VSG
Entry DOI | 10.2210/pdb2vsg/pdb |
Related | 1VSG |
Descriptor | VARIANT SURFACE GLYCOPROTEIN ILTAT 1.24 (2 entities in total) |
Functional Keywords | vsg, trypanosome, antigenic variation, membrane protein |
Biological source | Trypanosoma brucei |
Cellular location | Cell membrane; Lipid-anchor, GPI-anchor: P26329 |
Total number of polymer chains | 2 |
Total formula weight | 76573.48 |
Authors | Blum, M.L.,Down, J.A.,Metcalf, P.,Freymann, D.M.,Wiley, D.C. (deposition date: 1998-11-19, release date: 1998-11-25, Last modification date: 2024-10-16) |
Primary citation | Blum, M.L.,Down, J.A.,Gurnett, A.M.,Carrington, M.,Turner, M.J.,Wiley, D.C. A structural motif in the variant surface glycoproteins of Trypanosoma brucei. Nature, 362:603-609, 1993 Cited by PubMed 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. PubMed: 8464512DOI: 10.1038/362603a0 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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