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About:
The Moraxella adhesin UspA1 binds to its human CEACAM1 receptor by a deformable trimeric coiled-coil
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schema:ScholarlyArticle
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wasabi.inria.fr
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Type:
Academic Article
research paper
schema:ScholarlyArticle
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type
Academic Article
research paper
schema:ScholarlyArticle
isDefinedBy
Covid-on-the-Web dataset
has title
The Moraxella adhesin UspA1 binds to its human CEACAM1 receptor by a deformable trimeric coiled-coil
Creator
Virji, Mumtaz
Agnew, Christopher
Borodina, Elena
Conners, Rebecca
Lammie, Donna
Wess, Timothy
Brady, R
Burton, Nicholas
Catto, Lucy
Clarke, Anthony
Daniell, Sarah
Hill, Darryl
Sessions, Richard
Source
PMC
abstract
Moraxella catarrhalis is a ubiquitous human-specific bacterium commonly associated with upper and lower respiratory tract infections, including otitis media, sinusitis and chronic obstructive pulmonary disease. The bacterium uses an autotransporter protein UspA1 to target an important human cellular receptor carcinoembryonic antigen-related cell adhesion molecule 1 (CEACAM1). Using X-ray crystallography, we show that the CEACAM1 receptor-binding region of UspA1 unusually consists of an extended, rod-like left-handed trimeric coiled-coil. Mutagenesis and binding studies of UspA1 and the N-domain of CEACAM1 have been used to delineate the interacting surfaces between ligand and receptor and guide assembly of the complex. However, solution scattering, molecular modelling and electron microscopy analyses all indicate that significant bending of the UspA1 coiled-coil stalk also occurs. This explains how UspA1 can engage CEACAM1 at a site far distant from its head group, permitting closer proximity of the respective cell surfaces during infection.
has issue date
2008-06-18
(
xsd:dateTime
)
bibo:doi
10.1038/emboj.2008.101
bibo:pmid
18497748
has license
cc-by-nc-nd
sha1sum (hex)
fa9460f462e92e3ccbecc0e9fe406b886b7c1e35
schema:url
https://doi.org/10.1038/emboj.2008.101
resource representing a document's title
The Moraxella adhesin UspA1 binds to its human CEACAM1 receptor by a deformable trimeric coiled-coil
has PubMed Central identifier
PMC2396876
has PubMed identifier
18497748
schema:publication
EMBO J
resource representing a document's body
covid:fa9460f462e92e3ccbecc0e9fe406b886b7c1e35#body_text
is
schema:about
of
named entity 'CELLULAR'
named entity 'DELINEATE'
named entity 'ASSEMBLY'
named entity 'GUIDE'
named entity 'N-DOMAIN'
named entity 'SITE'
named entity 'ELECTRON MICROSCOPY'
named entity 'HAVE'
named entity 'INTERACTING'
named entity 'LIGAND'
named entity 'RECEPTOR'
named entity 'CARCINOEMBRYONIC ANTIGEN-RELATED CELL ADHESION MOLECULE 1'
named entity 'LEFT'
named entity 'USES'
named entity 'TARGET'
named entity 'IMPORTANT'
named entity 'IS A'
named entity 'BACTERIUM'
named entity 'HEAD'
named entity 'UBIQUITOUS'
named entity 'commonly'
named entity 'sinusitis'
named entity 'adhesin'
named entity 'coiled-coil'
named entity 'deformable'
named entity 'trimeric'
named entity 'COILED-COIL'
covid:arg/fa9460f462e92e3ccbecc0e9fe406b886b7c1e35
named entity 'COMPLEX'
named entity 'CHRONIC OBSTRUCTIVE PULMONARY DISEASE'
named entity 'X-RAY CRYSTALLOGRAPHY'
named entity 'SOLUTION'
named entity 'BINDS'
named entity 'CEACAM1'
named entity 'FAR'
named entity 'INCLUDING'
named entity 'CELL'
named entity 'PROTEIN '
named entity 'MORAXELLA'
named entity 'ADHESIN'
named entity 'RECEPTOR'
named entity 'ITS'
named entity 'MOLECULAR MODELLING'
named entity 'STUDIES'
named entity 'SPECIFIC'
named entity 'BINDING REGION'
named entity 'STALK'
named entity 'SIGNIFICANT'
named entity 'HOW'
named entity 'USED'
named entity 'SCATTERING'
named entity 'ASSOCIATED WITH'
named entity 'HUMAN'
named entity 'MORAXELLA CATARRHALIS'
named entity 'DISTANT FROM'
named entity 'COILED-COIL'
named entity 'INFECTION'
named entity 'ROD-LIKE'
named entity 'SURFACES'
named entity 'GROUP'
named entity 'EXTENDED'
named entity 'LOWER RESPIRATORY TRACT INFECTIONS'
named entity 'OTITIS MEDIA'
named entity 'PROXIMITY'
named entity 'HUMAN'
named entity 'UPPER'
named entity 'SINUSITIS'
named entity 'BINDING'
named entity 'ENGAGE'
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