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1o70

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[[Image:1o70.gif|left|200px]]<br />
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[[Image:1o70.gif|left|200px]]<br /><applet load="1o70" size="450" color="white" frame="true" align="right" spinBox="true"
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<applet load="1o70" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1o70, resolution 2.60&Aring;" />
caption="1o70, resolution 2.60&Aring;" />
'''NOVEL FOLD REVEALED BY THE STRUCTURE OF A FAS1 DOMAIN PAIR FROM THE INSECT CELL ADHESION MOLECULE FASCICLIN I'''<br />
'''NOVEL FOLD REVEALED BY THE STRUCTURE OF A FAS1 DOMAIN PAIR FROM THE INSECT CELL ADHESION MOLECULE FASCICLIN I'''<br />
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==About this Structure==
==About this Structure==
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1O70 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1O70 OCA].
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1O70 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=AC1:So4 Binding Site For Chain A'>AC1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1O70 OCA].
==Reference==
==Reference==
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[[Category: genetic disorder]]
[[Category: genetic disorder]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 16:45:05 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 16:51:50 2007''

Revision as of 14:42, 18 December 2007


1o70, resolution 2.60Å

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NOVEL FOLD REVEALED BY THE STRUCTURE OF A FAS1 DOMAIN PAIR FROM THE INSECT CELL ADHESION MOLECULE FASCICLIN I

Overview

Fasciclin I is an insect neural cell adhesion molecule consisting of four, FAS1 domains, homologs of which are present in many bacterial, plant, and, animal proteins. The crystal structure of FAS1 domains 3 and 4 of, Drosophila fasciclin I reveals a novel domain fold, consisting of a, seven-stranded beta wedge and a number of alpha helices. The two domains, are arranged in a linear fashion and interact through a substantial polar, interface. Missense mutations in the FAS1 domains of the human protein, betaig-h3 cause corneal dystrophies. Many mutations alter highly conserved, core residues, but the two most common mutations, affecting Arg-124 and, Arg-555, map to exposed alpha-helical regions, suggesting reduced protein, solubility as the disease mechanism.

About this Structure

1O70 is a Single protein structure of sequence from Drosophila melanogaster with SO4 as ligand. Known structural/functional Site: . Full crystallographic information is available from OCA.

Reference

Novel fold revealed by the structure of a FAS1 domain pair from the insect cell adhesion molecule fasciclin I., Clout NJ, Tisi D, Hohenester E, Structure. 2003 Feb;11(2):197-203. PMID:12575939

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