2om5: Difference between revisions

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[[Image:2om5.png|left|200px]]

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~~'''~~N-Terminal Fragment of Human TAX1~~'''~~

===N-Terminal Fragment of Human TAX1===

~~==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.~~

The line below this paragraph, {{ABSTRACT_PUBMED_17766378}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 17766378 is the PubMed ID number.

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==About this Structure==

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[[Category: Membrane protein]]

[[Category: X-ray crystallography]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sun May 4 11~~:11:50 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 00:03:46 2008''

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-[[Image:2om5.jpg|left|200px]]
+{{Seed}}
+[[Image:2om5.png|left|200px]]
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 {{STRUCTURE_2om5|  PDB=2om5  |  SCENE=  }}
-'''N-Terminal Fragment of Human TAX1'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_17766378}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17766378 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_17766378}}
 ==About this Structure==
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 [[Category: Membrane protein]]
 [[Category: X-ray crystallography]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 11:11:50 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 00:03:46 2008''