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PDBsum entry 1dab
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Cell adhesion
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PDB id
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1dab
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Structure of bordetella pertussis virulence factor p.69 pertactin.
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Authors
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P.Emsley,
I.G.Charles,
N.F.Fairweather,
N.W.Isaacs.
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Ref.
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Nature, 1996,
381,
90-92.
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PubMed id
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Abstract
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A new generation of whooping-cough vaccines contain P.69 pertactin, a
surface-exposed domain of an outer membrane protein expressed by the virulent
bacterium Bordetella pertussis. This protein is a virulence factor that mediates
adhesion to target mammalian cells, a reaction that is in part mediated by an
RGD sequence. The X-ray crystal structure of P.69 pertactin has been determined
to 2.5 A. The protein fold consists of a 16-stranded parallel beta-helix with a
V-shaped cross-section, and is the largest beta-helix known to date. Several
between-strand weakly conserved amino-acid repeats form internal and external
ladders. The structure appears as a helix from which several loops protrude,
which contain sequence motifs associated with the biological activity of the
protein. One particular (GGXXP)5 sequence is located directly after the RGD
motif, and may mediate interaction with epithelial cells. The carboxy-terminal
region of P.69 pertactin incorporates a (PQP)5 motif loop containing the major
immunoprotective epitope.
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