2om5: Difference between revisions
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{{STRUCTURE_2om5| PDB=2om5 | SCENE= }} | |||
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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.]] | ||
[[Category: | [[Category: Cell adhesion]] | ||
[[Category: | [[Category: Fibronectin]] | ||
[[Category: | [[Category: Ig-like c2-type]] | ||
[[Category: | [[Category: Immunoglobulin superfamily]] | ||
[[Category: | [[Category: Membrane protein]] | ||
[[Category: | [[Category: X-ray crystallography]] | ||
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Revision as of 08:11, 4 May 2008
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
