1xu6
From Proteopedia
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| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1xu6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xu6 OCA], [http://www.ebi.ac.uk/pdbsum/1xu6 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1xu6 RCSB]</span> | ||
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[[Category: cysteine knot]] | [[Category: cysteine knot]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:54:41 2008'' |
Revision as of 21:54, 30 March 2008
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of the C-terminal domain from Trypanosoma brucei Variant Surface Glycoprotein MITat1.2
Overview
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.
About this Structure
1XU6 is a Single protein structure of sequence from Trypanosoma brucei brucei. Full crystallographic information is available from OCA.
Reference
Structure of the C-terminal domain from Trypanosoma brucei variant surface glycoprotein MITat1.2., Chattopadhyay A, Jones NG, Nietlispach D, Nielsen PR, Voorheis HP, Mott HR, Carrington M, J Biol Chem. 2005 Feb 25;280(8):7228-35. Epub 2004 Nov 22. PMID:15557330
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