Crystal structure of hemolin: a horseshoe shape with implications for homophilic adhesion.
Science
; 281(5379): 991-5, 1998 Aug 14.
Article
in En
| MEDLINE
| ID: mdl-9703515
ABSTRACT
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.
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Database:
MEDLINE
Main subject:
Proteins
/
Cell Adhesion
Type of study:
Prognostic_studies
Limits:
Animals
/
Humans
Language:
En
Year:
1998
Type:
Article