1bih

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(New page: 200px<br /><applet load="1bih" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bih, resolution 3.10&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1bih.gif|left|200px]]<br /><applet load="1bih" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1bih.gif|left|200px]]<br /><applet load="1bih" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1bih, resolution 3.10&Aring;" />
caption="1bih, resolution 3.10&Aring;" />
'''CRYSTAL STRUCTURE OF THE INSECT IMMUNE PROTEIN HEMOLIN: A NEW DOMAIN ARRANGEMENT WITH IMPLICATIONS FOR HOMOPHILIC ADHESION'''<br />
'''CRYSTAL STRUCTURE OF THE INSECT IMMUNE PROTEIN HEMOLIN: A NEW DOMAIN ARRANGEMENT WITH IMPLICATIONS FOR HOMOPHILIC ADHESION'''<br />
==Overview==
==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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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==
==About this Structure==
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1BIH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Hyalophora_cecropia Hyalophora cecropia] with PO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BIH OCA].
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1BIH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Hyalophora_cecropia Hyalophora cecropia] with <scene name='pdbligand=PO4:'>PO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BIH OCA].
==Reference==
==Reference==
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[[Category: Hyalophora cecropia]]
[[Category: Hyalophora cecropia]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Bjorkman, P.J.]]
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[[Category: Bjorkman, P J.]]
[[Category: Faye, I.]]
[[Category: Faye, I.]]
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[[Category: Gastinel, L.N.]]
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[[Category: Gastinel, L N.]]
[[Category: Poon, P.]]
[[Category: Poon, P.]]
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[[Category: Su, X.D.]]
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[[Category: Su, X D.]]
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[[Category: Vaughn, D.E.]]
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[[Category: Vaughn, D E.]]
[[Category: PO4]]
[[Category: PO4]]
[[Category: homophilic adhesion]]
[[Category: homophilic adhesion]]
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[[Category: lps-binding]]
[[Category: lps-binding]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:40:48 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:55:39 2008''

Revision as of 09:55, 21 February 2008


1bih, resolution 3.10Å

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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 with as ligand. 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 Feb 21 11:55:39 2008

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