1bih
From Proteopedia
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| - | [[Image:1bih.gif|left|200px]] | + | [[Image:1bih.gif|left|200px]] |
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| - | '''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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| , resolution 3.10Å | |||||||
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| 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
Page seeded by OCA on Thu Mar 20 10:11:26 2008
