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Structure of a glycosylphosphatidylinositol-anchored domain from a trypanosome variant surface glycoprotein.

The cell surface of African trypanosomes is covered by a densely packed monolayer of a single protein, the variant surface glycoprotein (VSG). The VSG protects the trypanosome cell surface from effector molecules of the host immune system and is the mediator of antigenic variation. The sequence dive...

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Main Authors: Jones, Nicola G., Nietlispach, Daniel, Kumar Sharma, Reuben Sunil, Burke, David F., Eyres, Isobel, Mues, Marsilius, Mott, Helen R., Carrington, Mark
Format: Article
Language:English
English
Published: American Society for Biochemistry and Molecular Biology 2008
Online Access:http://psasir.upm.edu.my/id/eprint/16872/1/Structure%20of%20a%20glycosylphosphatidylinositol.pdf
http://psasir.upm.edu.my/id/eprint/16872/
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spelling my.upm.eprints.168722015-10-20T01:26:43Z http://psasir.upm.edu.my/id/eprint/16872/ Structure of a glycosylphosphatidylinositol-anchored domain from a trypanosome variant surface glycoprotein. Jones, Nicola G. Nietlispach, Daniel Kumar Sharma, Reuben Sunil Burke, David F. Eyres, Isobel Mues, Marsilius Mott, Helen R. Carrington, Mark The cell surface of African trypanosomes is covered by a densely packed monolayer of a single protein, the variant surface glycoprotein (VSG). The VSG protects the trypanosome cell surface from effector molecules of the host immune system and is the mediator of antigenic variation. The sequence divergence between VSGs that is necessary for antigenic variation can only occur within the constraints imposed by the structural features necessary to form the monolayer barrier. Here, the structures of the two domains that together comprise the C-terminal di-domain of VSG ILTat1.24 have been determined. The first domain has a structure similar to the single C-terminal domain of VSG MITat1.2 and provides proof of structural conservation in VSG C-terminal domains complementing the conservation of structure present in the N-terminal domain. The second domain, although based on the same fold, is a minimized version missing several structural features. The structure of the second domain contains the C-terminal residue that in the native VSG is attached to a glycosylphosphatidylinositol (GPI) anchor that retains the VSG on the external face of the plasma membrane. The solution structures of this domain and a VSG GPI glycan have been combined to produce the first structure-based model of a GPI-anchored protein. The model suggests that the core glycan of the GPI anchor lies in a groove on the surface of the domain and that there is a close association between the GPI glycan and protein. More widely, the GPI glycan may be an integral part of the structure of other GPI-anchored proteins. American Society for Biochemistry and Molecular Biology 2008 Article PeerReviewed application/pdf en http://psasir.upm.edu.my/id/eprint/16872/1/Structure%20of%20a%20glycosylphosphatidylinositol.pdf Jones, Nicola G. and Nietlispach, Daniel and Kumar Sharma, Reuben Sunil and Burke, David F. and Eyres, Isobel and Mues, Marsilius and Mott, Helen R. and Carrington, Mark (2008) Structure of a glycosylphosphatidylinositol-anchored domain from a trypanosome variant surface glycoprotein. Journal of Biological Chemistry, 283 (6). pp. 3584-3593. ISSN 0021-9258; ESSN: 1083-351X 10.1074/jbc.M706207200 English
institution Universiti Putra Malaysia
building UPM Library
collection Institutional Repository
continent Asia
country Malaysia
content_provider Universiti Putra Malaysia
content_source UPM Institutional Repository
url_provider http://psasir.upm.edu.my/
language English
English
description The cell surface of African trypanosomes is covered by a densely packed monolayer of a single protein, the variant surface glycoprotein (VSG). The VSG protects the trypanosome cell surface from effector molecules of the host immune system and is the mediator of antigenic variation. The sequence divergence between VSGs that is necessary for antigenic variation can only occur within the constraints imposed by the structural features necessary to form the monolayer barrier. Here, the structures of the two domains that together comprise the C-terminal di-domain of VSG ILTat1.24 have been determined. The first domain has a structure similar to the single C-terminal domain of VSG MITat1.2 and provides proof of structural conservation in VSG C-terminal domains complementing the conservation of structure present in the N-terminal domain. The second domain, although based on the same fold, is a minimized version missing several structural features. The structure of the second domain contains the C-terminal residue that in the native VSG is attached to a glycosylphosphatidylinositol (GPI) anchor that retains the VSG on the external face of the plasma membrane. The solution structures of this domain and a VSG GPI glycan have been combined to produce the first structure-based model of a GPI-anchored protein. The model suggests that the core glycan of the GPI anchor lies in a groove on the surface of the domain and that there is a close association between the GPI glycan and protein. More widely, the GPI glycan may be an integral part of the structure of other GPI-anchored proteins.
format Article
author Jones, Nicola G.
Nietlispach, Daniel
Kumar Sharma, Reuben Sunil
Burke, David F.
Eyres, Isobel
Mues, Marsilius
Mott, Helen R.
Carrington, Mark
spellingShingle Jones, Nicola G.
Nietlispach, Daniel
Kumar Sharma, Reuben Sunil
Burke, David F.
Eyres, Isobel
Mues, Marsilius
Mott, Helen R.
Carrington, Mark
Structure of a glycosylphosphatidylinositol-anchored domain from a trypanosome variant surface glycoprotein.
author_facet Jones, Nicola G.
Nietlispach, Daniel
Kumar Sharma, Reuben Sunil
Burke, David F.
Eyres, Isobel
Mues, Marsilius
Mott, Helen R.
Carrington, Mark
author_sort Jones, Nicola G.
title Structure of a glycosylphosphatidylinositol-anchored domain from a trypanosome variant surface glycoprotein.
title_short Structure of a glycosylphosphatidylinositol-anchored domain from a trypanosome variant surface glycoprotein.
title_full Structure of a glycosylphosphatidylinositol-anchored domain from a trypanosome variant surface glycoprotein.
title_fullStr Structure of a glycosylphosphatidylinositol-anchored domain from a trypanosome variant surface glycoprotein.
title_full_unstemmed Structure of a glycosylphosphatidylinositol-anchored domain from a trypanosome variant surface glycoprotein.
title_sort structure of a glycosylphosphatidylinositol-anchored domain from a trypanosome variant surface glycoprotein.
publisher American Society for Biochemistry and Molecular Biology
publishDate 2008
url http://psasir.upm.edu.my/id/eprint/16872/1/Structure%20of%20a%20glycosylphosphatidylinositol.pdf
http://psasir.upm.edu.my/id/eprint/16872/
_version_ 1643826344250834944
score 13.211869

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