|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
5379
|
|
pubmed:dateCreated |
1998-8-25
|
|
pubmed:databankReference |
|
|
pubmed:abstractText |
Hemolin, an insect immunoglobulin superfamily member, is a lipopolysaccharide-binding immune protein induced during bacterial infection. The 3.1 angstrom crystal structure reveals a bound phosphate and patches of positive charge, which may represent the lipopolysaccharide binding site, and a new and unexpected arrangement of four immunoglobulin-like domains forming a horseshoe. Sequence analysis and analytical ultracentrifugation suggest that the domain arrangement is a feature of the L1 family of neural cell adhesion molecules related to hemolin. These results are relevant to interpretation of human L1 mutations in neurological diseases and suggest a domain swapping model for how L1 family proteins mediate homophilic adhesion.
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cell Adhesion Molecules, Neuronal,
http://linkedlifedata.com/resource/pubmed/chemical/Drosophila Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulins,
http://linkedlifedata.com/resource/pubmed/chemical/Insect Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Leukocyte L1 Antigen Complex,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Neural Cell Adhesion Molecules,
http://linkedlifedata.com/resource/pubmed/chemical/Nrg protein, Drosophila,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/hemolin
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Aug
|
|
pubmed:issn |
0036-8075
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
14
|
|
pubmed:volume |
281
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
991-5
|
|
pubmed:dateRevised |
2007-3-19
|
|
pubmed:meshHeading |
pubmed-meshheading:9703515-Amino Acid Sequence,
pubmed-meshheading:9703515-Animals,
pubmed-meshheading:9703515-Cell Adhesion,
pubmed-meshheading:9703515-Cell Adhesion Molecules, Neuronal,
pubmed-meshheading:9703515-Crystallography, X-Ray,
pubmed-meshheading:9703515-Drosophila Proteins,
pubmed-meshheading:9703515-Drosophila melanogaster,
pubmed-meshheading:9703515-Humans,
pubmed-meshheading:9703515-Immunoglobulins,
pubmed-meshheading:9703515-Insect Proteins,
pubmed-meshheading:9703515-Leukocyte L1 Antigen Complex,
pubmed-meshheading:9703515-Membrane Glycoproteins,
pubmed-meshheading:9703515-Models, Molecular,
pubmed-meshheading:9703515-Molecular Sequence Data,
pubmed-meshheading:9703515-Moths,
pubmed-meshheading:9703515-Neural Cell Adhesion Molecules,
pubmed-meshheading:9703515-Protein Binding,
pubmed-meshheading:9703515-Protein Conformation,
pubmed-meshheading:9703515-Proteins,
pubmed-meshheading:9703515-Recombinant Proteins,
pubmed-meshheading:9703515-Sequence Homology, Amino Acid
|
|
pubmed:year |
1998
|
|
pubmed:articleTitle |
Crystal structure of hemolin: a horseshoe shape with implications for homophilic adhesion.
|
|
pubmed:affiliation |
Division of Biology 156-29 and Howard Hughes Medical Institute, California Institute of Technology, Pasadena, CA 91125, USA.
|
|
pubmed:publicationType |
Journal Article
|
