1bih
From Proteopedia
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|PDB= 1bih |SIZE=350|CAPTION= <scene name='initialview01'>1bih</scene>, resolution 3.10Å | |PDB= 1bih |SIZE=350|CAPTION= <scene name='initialview01'>1bih</scene>, resolution 3.10Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=PO4:PHOSPHATE ION'>PO4</scene> | + | |LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bih FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bih OCA], [http://www.ebi.ac.uk/pdbsum/1bih PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1bih RCSB]</span> | ||
}} | }} | ||
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[[Category: Su, X D.]] | [[Category: Su, X D.]] | ||
[[Category: Vaughn, D E.]] | [[Category: Vaughn, D E.]] | ||
| - | [[Category: PO4]] | ||
[[Category: homophilic adhesion]] | [[Category: homophilic adhesion]] | ||
[[Category: insect immunity]] | [[Category: insect immunity]] | ||
[[Category: lps-binding]] | [[Category: lps-binding]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:01:35 2008'' |
Revision as of 16:01, 30 March 2008
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| , resolution 3.10Å | |||||||
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| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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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