1bih: Difference between revisions

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{{STRUCTURE_1bih|  PDB=1bih  |  SCENE=  }}  
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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===




==Overview==
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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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==About this Structure==
==About this Structure==
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[[Category: Insect immunity]]
[[Category: Insect immunity]]
[[Category: Lps-binding]]
[[Category: Lps-binding]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:12:59 2008''

Revision as of 16:13, 30 June 2008

File:1bih.png

Template:STRUCTURE 1bih

CRYSTAL STRUCTURE OF THE INSECT IMMUNE PROTEIN HEMOLIN: A NEW DOMAIN ARRANGEMENT WITH IMPLICATIONS FOR HOMOPHILIC ADHESION

Template:ABSTRACT PUBMED 9703515

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

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