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'''CRYSTAL STRUCTURE OF THE INSECT IMMUNE PROTEIN HEMOLIN: A NEW DOMAIN ARRANGEMENT WITH IMPLICATIONS FOR HOMOPHILIC ADHESION''' | '''CRYSTAL STRUCTURE OF THE INSECT IMMUNE PROTEIN HEMOLIN: A NEW DOMAIN ARRANGEMENT WITH IMPLICATIONS FOR HOMOPHILIC ADHESION''' | ||
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[[Category: Su, X D.]] | [[Category: Su, X D.]] | ||
[[Category: Vaughn, D E.]] | [[Category: Vaughn, D E.]] | ||
[[Category: | [[Category: Homophilic adhesion]] | ||
[[Category: | [[Category: Insect immunity]] | ||
[[Category: | [[Category: Lps-binding]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:33:11 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 08:33, 2 May 2008
CRYSTAL STRUCTURE OF THE INSECT IMMUNE PROTEIN HEMOLIN: A NEW DOMAIN ARRANGEMENT WITH IMPLICATIONS FOR HOMOPHILIC ADHESION
Overview
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.
About this Structure
1BIH is a Single protein structure of sequence from Hyalophora cecropia. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Fri May 2 11:33:11 2008
