1xu6: Difference between revisions

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[[Image:1xu6.gif|left|200px]]
[[Image:1xu6.gif|left|200px]]


{{Structure
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'''Structure of the C-terminal domain from Trypanosoma brucei Variant Surface Glycoprotein MITat1.2'''
'''Structure of the C-terminal domain from Trypanosoma brucei Variant Surface Glycoprotein MITat1.2'''
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[[Category: Nietlispach, D.]]
[[Category: Nietlispach, D.]]
[[Category: Voorheis, H P.]]
[[Category: Voorheis, H P.]]
[[Category: cysteine knot]]
[[Category: Cysteine knot]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 15:30:51 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:54:41 2008''

Revision as of 15:30, 3 May 2008

File:1xu6.gif

Template:STRUCTURE 1xu6

Structure of the C-terminal domain from Trypanosoma brucei Variant Surface Glycoprotein MITat1.2


OverviewOverview

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 StructureAbout this Structure

1XU6 is a Single protein structure of sequence from Trypanosoma brucei brucei. Full crystallographic information is available from OCA.

ReferenceReference

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 Page seeded by OCA on Sat May 3 15:30:51 2008

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