1o70
From Proteopedia
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|PDB= 1o70 |SIZE=350|CAPTION= <scene name='initialview01'>1o70</scene>, resolution 2.60Å | |PDB= 1o70 |SIZE=350|CAPTION= <scene name='initialview01'>1o70</scene>, resolution 2.60Å | ||
|SITE= <scene name='pdbsite=AC1:So4+Binding+Site+For+Chain+A'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:So4+Binding+Site+For+Chain+A'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | + | |LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1o70 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o70 OCA], [http://www.ebi.ac.uk/pdbsum/1o70 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1o70 RCSB]</span> | ||
}} | }} | ||
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[[Category: Hohenester, E.]] | [[Category: Hohenester, E.]] | ||
[[Category: Tisi, D.]] | [[Category: Tisi, D.]] | ||
| - | [[Category: SO4]] | ||
[[Category: axon guidance]] | [[Category: axon guidance]] | ||
[[Category: cell adhesion]] | [[Category: cell adhesion]] | ||
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[[Category: genetic disorder]] | [[Category: genetic disorder]] | ||
| - | ''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 22:40:46 2008'' |
Revision as of 19:40, 30 March 2008
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| , resolution 2.60Å | |||||||
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| Sites: | |||||||
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
Page seeded by OCA on Sun Mar 30 22:40:46 2008
