2om5: Difference between revisions

Revision as of 19:20, 21 February 2008

N-Terminal Fragment of Human TAX1

OverviewOverview

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 StructureAbout this Structure

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

ReferenceReference

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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OCA

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 ==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.
+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==
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 [[Category: x-ray crystallography; ig-like c2-type; immunoglobulin superfamily; fibronectin; membrane protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 12:09:10 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:20:02 2008''