1osp
From Proteopedia
(New page: 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=" | + | |
caption="1osp, resolution 1.95Å" /> | caption="1osp, resolution 1.95Å" /> | ||
'''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 | + | 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:// | + | 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 | + | [[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 | + | [[Category: outer surface protein a complexed with fab184 1]] |
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:21:08 2008'' |
Revision as of 12:21, 21 February 2008
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CRYSTAL STRUCTURE OF OUTER SURFACE PROTEIN A OF BORRELIA BURGDORFERI COMPLEXED WITH A MURINE MONOCLONAL ANTIBODY FAB
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.
About this Structure
1OSP is a Protein complex structure of sequences from Borrelia burgdorferi and Mus musculus. Full crystallographic information is available from OCA.
Reference
Crystal structure of Lyme disease antigen outer surface protein A complexed with an Fab., Li H, Dunn JJ, Luft BJ, Lawson CL, Proc Natl Acad Sci U S A. 1997 Apr 15;94(8):3584-9. PMID:9108020
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