1bih: Difference between revisions
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[[Image:1bih.gif|left|200px]] | [[Image:1bih.gif|left|200px]] | ||
'''CRYSTAL STRUCTURE OF THE INSECT IMMUNE PROTEIN HEMOLIN: A NEW DOMAIN ARRANGEMENT WITH IMPLICATIONS FOR HOMOPHILIC ADHESION''' | {{Structure | ||
|PDB= 1bih |SIZE=350|CAPTION= <scene name='initialview01'>1bih</scene>, resolution 3.10Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=PO4:PHOSPHATE ION'>PO4</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''CRYSTAL STRUCTURE OF THE INSECT IMMUNE PROTEIN HEMOLIN: A NEW DOMAIN ARRANGEMENT WITH IMPLICATIONS FOR HOMOPHILIC ADHESION''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1BIH is a [ | 1BIH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Hyalophora_cecropia Hyalophora cecropia]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BIH OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9703515 9703515] | ||
[[Category: Hyalophora cecropia]] | [[Category: Hyalophora cecropia]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: lps-binding]] | [[Category: lps-binding]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:11:26 2008'' | ||
Revision as of 08:11, 20 March 2008
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| 1bih, resolution 3.10Å | |||||||||||||
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| Ligands: | PO4 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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
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