2jwg

Structure of a Glycosylphosphatidylinositol-anchored Domain from a Trypanosome Variant Surface GlycoproteinStructure of a Glycosylphosphatidylinositol-anchored Domain from a Trypanosome Variant Surface Glycoprotein

Structural highlights 2jwg is a 1 chain structure with sequence from Trypanosoma brucei brucei. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR, 35 models Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function VSI4_TRYBB VSG forms a coat on the surface of the parasite. The trypanosome evades the immune response of the host by expressing a series of antigenically distinct VSGs from an estimated 1000 VSG genes. Publication Abstract from PubMed 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. Structure of a glycosylphosphatidylinositol-anchored domain from a trypanosome variant surface glycoprotein.,Jones NG, Nietlispach D, Sharma R, Burke DF, Eyres I, Mues M, Mott HR, Carrington M J Biol Chem. 2008 Feb 8;283(6):3584-93. Epub 2007 Nov 14. PMID:18003615 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

spinqualitylabelsall models 2jwg Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image