2om5
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(New page: 200px<br /><applet load="2om5" size="350" color="white" frame="true" align="right" spinBox="true" caption="2om5, resolution 3.07Å" /> '''N-Terminal Fragment ...)
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Revision as of 10:09, 23 January 2008
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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
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