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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
11
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pubmed:dateCreated |
2000-12-8
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pubmed:databankReference |
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pubmed:abstractText |
The coxsackievirus and adenovirus receptor (CAR) comprises two extracellular immunoglobulin domains, a transmembrane helix and a C-terminal intracellular domain. The amino-terminal immunoglobulin domain (D1) of CAR is necessary and sufficient for adenovirus binding, whereas the site of coxsackievirus attachment has not yet been localized. The normal cellular role of CAR is currently unknown, although CAR was recently proposed to function as a homophilic cell adhesion molecule.
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pubmed:grant |
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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0969-2126
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
8
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1147-55
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pubmed:dateRevised |
2011-7-1
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pubmed:meshHeading |
pubmed-meshheading:11080637-Adenoviruses, Human,
pubmed-meshheading:11080637-Amino Acid Sequence,
pubmed-meshheading:11080637-Animals,
pubmed-meshheading:11080637-Crystallography, X-Ray,
pubmed-meshheading:11080637-Dimerization,
pubmed-meshheading:11080637-Enterovirus,
pubmed-meshheading:11080637-Humans,
pubmed-meshheading:11080637-Hydrogen Bonding,
pubmed-meshheading:11080637-Mice,
pubmed-meshheading:11080637-Models, Molecular,
pubmed-meshheading:11080637-Molecular Sequence Data,
pubmed-meshheading:11080637-Protein Conformation,
pubmed-meshheading:11080637-Protein Multimerization,
pubmed-meshheading:11080637-Protein Structure, Tertiary,
pubmed-meshheading:11080637-Receptors, Virus,
pubmed-meshheading:11080637-Recombinant Fusion Proteins,
pubmed-meshheading:11080637-Sequence Alignment,
pubmed-meshheading:11080637-Sequence Homology, Amino Acid,
pubmed-meshheading:11080637-Solubility,
pubmed-meshheading:11080637-Structure-Activity Relationship,
pubmed-meshheading:11080637-Ultracentrifugation
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pubmed:year |
2000
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pubmed:articleTitle |
Dimeric structure of the coxsackievirus and adenovirus receptor D1 domain at 1.7 A resolution.
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pubmed:affiliation |
European Molecular Biology Laboratory Grenoble Outstation c/o Institut Laue Langevin BP 156 F-38042 9, Grenoble Cedex, France. m.vanraaij@chem.leidenuniv.nl
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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