2om5

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[[Image:2om5.jpg|left|200px]]
[[Image:2om5.jpg|left|200px]]
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{{Structure
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|PDB= 2om5 |SIZE=350|CAPTION= <scene name='initialview01'>2om5</scene>, resolution 3.07&Aring;
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The line below this paragraph, containing "STRUCTURE_2om5", creates the "Structure Box" on the page.
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|SITE=
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|GENE= CNTN2, TAG1, TAX ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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|DOMAIN=
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{{STRUCTURE_2om5| PDB=2om5 | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2om5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2om5 OCA], [http://www.ebi.ac.uk/pdbsum/2om5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2om5 RCSB]</span>
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'''N-Terminal Fragment of Human TAX1'''
'''N-Terminal Fragment of Human TAX1'''
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[[Category: Sonderegger, P.]]
[[Category: Sonderegger, P.]]
[[Category: Welte, W.]]
[[Category: Welte, W.]]
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[[Category: cell adhesion]]
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[[Category: Cell adhesion]]
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[[Category: fibronectin]]
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[[Category: Fibronectin]]
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[[Category: ig-like c2-type]]
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[[Category: Ig-like c2-type]]
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[[Category: immunoglobulin superfamily]]
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[[Category: Immunoglobulin superfamily]]
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[[Category: membrane protein]]
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[[Category: Membrane protein]]
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[[Category: x-ray crystallography]]
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[[Category: X-ray crystallography]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 11:11:50 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:19:55 2008''
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Revision as of 08:11, 4 May 2008

Template:STRUCTURE 2om5

N-Terminal Fragment of Human TAX1


Overview

Human TAG-1 is a neural cell adhesion molecule that is crucial for the development of the nervous system during embryogenesis. It consists of six immunoglobulin-like and four fibronectin III-like domains and is anchored to the membrane by glycosylphosphatidylinositol. Herein we present the crystal structure of the four N-terminal immunoglobulin-like domains of TAG-1 (TAG-1(Ig1-4)), known to be important in heterophilic and homophilic macromolecular interactions. The contacts of neighboring molecules within the crystal were investigated. A comparison with the structure of the chicken ortholog resulted in an alternative mode for the molecular mechanism of homophilic TAG-1 interaction. This mode of TAG-1 homophilic interaction is based on dimer formation rather than formation of a molecular zipper as proposed for the chicken ortholog.

About this Structure

2OM5 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

The crystal structure of the ligand-binding module of human TAG-1 suggests a new mode of homophilic interaction., Mortl M, Sonderegger P, Diederichs K, Welte W, Protein Sci. 2007 Oct;16(10):2174-83. Epub 2007 Aug 31. PMID:17766378 Page seeded by OCA on Sun May 4 11:11:50 2008

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