1XU6
Structure of the C-terminal domain from Trypanosoma brucei Variant Surface Glycoprotein MITat1.2
Summary for 1XU6
| Entry DOI | 10.2210/pdb1xu6/pdb |
| NMR Information | BMRB: 6419 |
| Descriptor | Variant surface glycoprotein MITAT 1.2 (1 entity in total) |
| Functional Keywords | cysteine knot, immune system, membrane protein |
| Biological source | Trypanosoma |
| Cellular location | Cell membrane; Lipid-anchor, GPI-anchor: P26332 |
| Total number of polymer chains | 1 |
| Total formula weight | 8750.56 |
| Authors | Chattopadhyay, A.,Jones, N.G.,Nietlispach, D.,Nielsen, P.R.,Voorheis, H.P.,Mott, H.R.,Carrington, M. (deposition date: 2004-10-25, release date: 2004-11-30, Last modification date: 2024-10-30) |
| Primary citation | Chattopadhyay, A.,Jones, N.G.,Nietlispach, D.,Nielsen, P.R.,Voorheis, H.P.,Mott, H.R.,Carrington, M. Structure of the C-terminal domain from Trypanosoma brucei variant surface glycoprotein MITat1.2 J.Biol.Chem., 280:7228-7235, 2004 Cited by PubMed Abstract: The variant surface glycoprotein (VSG) of African trypanosomes has a structural role in protecting other cell surface proteins from effector molecules of the mammalian immune system and also undergoes antigenic variation necessary for a persistent infection in a host. Here we have reported the solution structure of a VSG type 2 C-terminal domain from MITat1.2, completing the first structure of both domains of a VSG. The isolated C-terminal domain is a monomer in solution and forms a novel fold, which commences with a short alpha-helix followed by a single turn of 3(10)-helix and connected by a short loop to a small anti-parallel beta-sheet and then a longer alpha-helix at the C terminus. This compact domain is flanked by two unstructured regions. The structured part of the domain contains 42 residues, and the core comprises 2 disulfide bonds and 2 hydrophobic residues. These cysteines and hydrophobic residues are conserved in other VSGs, and we have modeled the structures of two further VSG C-terminal domains using the structure of MITat1.2. The models suggest that the overall structure of the core is conserved in the different VSGs but that the C-terminal alpha-helix is of variable length and depends on the presence of charged residues. The results provided evidence for a conserved tertiary structure for all the type 2 VSG C-terminal domains, indicated that VSG dimers form through interactions between N-terminal domains, and showed that the selection pressure for sequence variation within a conserved tertiary structure acts on the whole of the VSG molecule. PubMed: 15557330DOI: 10.1074/jbc.M410787200 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
