2om5

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{{STRUCTURE_2om5| PDB=2om5 | SCENE= }}
{{STRUCTURE_2om5| PDB=2om5 | SCENE= }}
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'''N-Terminal Fragment of Human TAX1'''
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===N-Terminal Fragment of Human TAX1===
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==Overview==
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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.
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==About this Structure==
==About this Structure==
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[[Category: Membrane protein]]
[[Category: Membrane protein]]
[[Category: X-ray crystallography]]
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Revision as of 21:03, 28 July 2008

Image:2om5.png

Template:STRUCTURE 2om5

N-Terminal Fragment of Human TAX1

Template:ABSTRACT PUBMED 17766378

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

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