1dab

<table><tr><td colspan='2'>[[1dab]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacterium_tussis-convulsivae"_lehmann_and_neumann_1927 "bacterium tussis-convulsivae" lehmann and neumann 1927]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DAB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DAB FirstGlance]. <br>

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1dab FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dab OCA], [https://pdbe.org/1dab PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dab RCSB], [https://www.ebi.ac.uk/pdbsum/1dab PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dab ProSAT]</span></td></tr>

[[https://www.uniprot.org/uniprot/PERT_BORPE PERT_BORPE]] Agglutinogen that binds to eukaryotic cells; a process mediated by the R-G-D sequence. Pertactin may have a role in bacterial adhesion, and thus play a role in virulence. May contribute to the disease state of whooping cough.

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== Publication Abstract from PubMed ==

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.

Structure of Bordetella pertussis virulence factor P.69 pertactin.,Emsley P, Charles IG, Fairweather NF, Isaacs NW Nature. 1996 May 2;381(6577):90-2. PMID:8609998<ref>PMID:8609998</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Bacterium tussis-convulsivae lehmann and neumann 1927]]

[[Category: Charles, I G]]

[[Category: Emsley, P]]

[[Category: Fairweather, N F]]

[[Category: Isaacs, N W]]

[[Category: Pertussis beta helix]]