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1g5z

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(New page: 200px<br /><applet load="1g5z" size="450" color="white" frame="true" align="right" spinBox="true" caption="1g5z, resolution 2.51&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1g5z.jpg|left|200px]]<br /><applet load="1g5z" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1g5z, resolution 2.51&Aring;" />
caption="1g5z, resolution 2.51&Aring;" />
'''CRYSTAL STRUCTURE OF LYME DISEASE ANTIGEN OUTER SURFACE PROTEIN C (OSPC) FROM BORRELIA BURGDORFERI STRAIN N40'''<br />
'''CRYSTAL STRUCTURE OF LYME DISEASE ANTIGEN OUTER SURFACE PROTEIN C (OSPC) FROM BORRELIA BURGDORFERI STRAIN N40'''<br />
==Overview==
==Overview==
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The outer surface protein C (OspC) is one of the major host-induced, antigens of Borrelia burgdorferi, the causative agent of Lyme disease. We, have solved the crystal structure of recombinant OspC to a resolution of, 2.5 A. OspC, a largely alpha-helical protein, is a dimer with a, characteristic central four-helical bundle formed by association of the, two longest helices from each subunit. OspC is very different from OspA, and similar to the extracellular domain of the bacterial aspartate, receptor and the variant surface glycoprotein from Trypanosoma brucei., Most of the surface-exposed residues of OspC are highly variable among, different OspC isolates. The membrane proximal halves of the two long, alpha-helices are the only conserved regions that are solvent accessible., As vaccination with recombinant OspC has been shown to elicit a protective, immune response in mice, these regions are candidates for peptide-based, vaccines.
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The outer surface protein C (OspC) is one of the major host-induced antigens of Borrelia burgdorferi, the causative agent of Lyme disease. We have solved the crystal structure of recombinant OspC to a resolution of 2.5 A. OspC, a largely alpha-helical protein, is a dimer with a characteristic central four-helical bundle formed by association of the two longest helices from each subunit. OspC is very different from OspA and similar to the extracellular domain of the bacterial aspartate receptor and the variant surface glycoprotein from Trypanosoma brucei. Most of the surface-exposed residues of OspC are highly variable among different OspC isolates. The membrane proximal halves of the two long alpha-helices are the only conserved regions that are solvent accessible. As vaccination with recombinant OspC has been shown to elicit a protective immune response in mice, these regions are candidates for peptide-based vaccines.
==About this Structure==
==About this Structure==
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1G5Z is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Borrelia_burgdorferi Borrelia burgdorferi]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1G5Z OCA].
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1G5Z is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Borrelia_burgdorferi Borrelia burgdorferi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G5Z OCA].
==Reference==
==Reference==
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[[Category: Hook, M.]]
[[Category: Hook, M.]]
[[Category: Klabunde, T.]]
[[Category: Klabunde, T.]]
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[[Category: Owens, R.T.]]
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[[Category: Owens, R T.]]
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[[Category: Pikas, D.S.]]
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[[Category: Pikas, D S.]]
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[[Category: Sacchettini, J.C.]]
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[[Category: Sacchettini, J C.]]
[[Category: Sharma, V.]]
[[Category: Sharma, V.]]
[[Category: alpha helix protein]]
[[Category: alpha helix protein]]
[[Category: surface protein]]
[[Category: surface protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 00:53:58 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:46:30 2008''

Revision as of 10:46, 21 February 2008

Image:1g5z.jpg

1g5z, resolution 2.51Å

Drag the structure with the mouse to rotate

CRYSTAL STRUCTURE OF LYME DISEASE ANTIGEN OUTER SURFACE PROTEIN C (OSPC) FROM BORRELIA BURGDORFERI STRAIN N40

Overview

The outer surface protein C (OspC) is one of the major host-induced antigens of Borrelia burgdorferi, the causative agent of Lyme disease. We have solved the crystal structure of recombinant OspC to a resolution of 2.5 A. OspC, a largely alpha-helical protein, is a dimer with a characteristic central four-helical bundle formed by association of the two longest helices from each subunit. OspC is very different from OspA and similar to the extracellular domain of the bacterial aspartate receptor and the variant surface glycoprotein from Trypanosoma brucei. Most of the surface-exposed residues of OspC are highly variable among different OspC isolates. The membrane proximal halves of the two long alpha-helices are the only conserved regions that are solvent accessible. As vaccination with recombinant OspC has been shown to elicit a protective immune response in mice, these regions are candidates for peptide-based vaccines.

About this Structure

1G5Z is a Single protein structure of sequence from Borrelia burgdorferi. Full crystallographic information is available from OCA.

Reference

Crystal structure of Lyme disease antigen outer surface protein C from Borrelia burgdorferi., Eicken C, Sharma V, Klabunde T, Owens RT, Pikas DS, Hook M, Sacchettini JC, J Biol Chem. 2001 Mar 30;276(13):10010-5. Epub 2001 Jan 3. PMID:11139584

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