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New page: left|200px<br /> <applet load="1osp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1osp, resolution 1.95Å" /> '''CRYSTAL STRUCTURE O...
 
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[[Image:1osp.gif|left|200px]]<br />
[[Image:1osp.gif|left|200px]]<br /><applet load="1osp" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1osp" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1osp, resolution 1.95&Aring;" />
caption="1osp, resolution 1.95&Aring;" />
'''CRYSTAL STRUCTURE OF OUTER SURFACE PROTEIN A OF BORRELIA BURGDORFERI COMPLEXED WITH A MURINE MONOCLONAL ANTIBODY FAB'''<br />
'''CRYSTAL STRUCTURE OF OUTER SURFACE PROTEIN A OF BORRELIA BURGDORFERI COMPLEXED WITH A MURINE MONOCLONAL ANTIBODY FAB'''<br />


==Overview==
==Overview==
OspA (outer surface protein A) is an abundant immunogenic lipoprotein of, the Lyme disease spirochete Borrelia burgdorferi. The crystal structure of, a soluble recombinant form of OspA was solved in a complex with the Fab, fragment of mouse monoclonal antibody 184.1 and refined to a resolution of, 1.9 A. OspA has a repetitive antiparallel beta topology with an unusual, nonglobular region of "freestanding" sheet connecting globular N- and, C-terminal domains. Arrays of residues with alternating charges are a, predominant feature of the folding pattern in the nonglobular region. The, 184.1 epitope overlaps with a well conserved surface in the N-terminal, domain, and a hydrophobic cavity buried in a positively charged cleft in, the C-terminal domain is a potential binding site for an unknown ligand., An exposed variable region on the C-terminal domain of OspA is predicted, to be an important factor in the worldwide effectiveness of OspA-based, vaccines.
OspA (outer surface protein A) is an abundant immunogenic lipoprotein of the Lyme disease spirochete Borrelia burgdorferi. The crystal structure of a soluble recombinant form of OspA was solved in a complex with the Fab fragment of mouse monoclonal antibody 184.1 and refined to a resolution of 1.9 A. OspA has a repetitive antiparallel beta topology with an unusual nonglobular region of "freestanding" sheet connecting globular N- and C-terminal domains. Arrays of residues with alternating charges are a predominant feature of the folding pattern in the nonglobular region. The 184.1 epitope overlaps with a well conserved surface in the N-terminal domain, and a hydrophobic cavity buried in a positively charged cleft in the C-terminal domain is a potential binding site for an unknown ligand. An exposed variable region on the C-terminal domain of OspA is predicted to be an important factor in the worldwide effectiveness of OspA-based vaccines.


==About this Structure==
==About this Structure==
1OSP is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Borrelia_burgdorferi Borrelia burgdorferi] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OSP OCA].  
1OSP is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Borrelia_burgdorferi Borrelia burgdorferi] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OSP OCA].  


==Reference==
==Reference==
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Lawson, C.L.]]
[[Category: Lawson, C L.]]
[[Category: Li, H.]]
[[Category: Li, H.]]
[[Category: borrelia burgdorferi strain b31]]
[[Category: borrelia burgdorferi strain b31]]
[[Category: complex (immunoglobulin/lipoprotein)]]
[[Category: complex (immunoglobulin/lipoprotein)]]
[[Category: outer surface protein a complexed with fab184.1]]
[[Category: outer surface protein a complexed with fab184 1]]


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