2om5: Difference between revisions
New page: left|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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==Overview== | ==Overview== | ||
Human TAG-1 is a neural cell adhesion molecule that is crucial for the | 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== | ==About this Structure== | ||
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[[Category: x-ray crystallography; ig-like c2-type; immunoglobulin superfamily; fibronectin; membrane protein]] | [[Category: x-ray crystallography; ig-like c2-type; immunoglobulin superfamily; fibronectin; membrane protein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:20:02 2008'' |