Structural highlights
Function
[HEMO_HYACE] Insect-immune protein. Forms a protein complex at the bacterial surface. Can inhibit hemocyte aggregation.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Crystal structure of hemolin: a horseshoe shape with implications for homophilic adhesion.,Su XD, Gastinel LN, Vaughn DE, Faye I, Poon P, Bjorkman PJ Science. 1998 Aug 14;281(5379):991-5. PMID:9703515[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Su XD, Gastinel LN, Vaughn DE, Faye I, Poon P, Bjorkman PJ. Crystal structure of hemolin: a horseshoe shape with implications for homophilic adhesion. Science. 1998 Aug 14;281(5379):991-5. PMID:9703515
