2om5
From Proteopedia
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- | [[Image:2om5.jpg|left|200px]] | + | [[Image:2om5.jpg|left|200px]] |
- | + | ||
- | '''N-Terminal Fragment of Human TAX1''' | + | {{Structure |
+ | |PDB= 2om5 |SIZE=350|CAPTION= <scene name='initialview01'>2om5</scene>, resolution 3.07Å | ||
+ | |SITE= | ||
+ | |LIGAND= | ||
+ | |ACTIVITY= | ||
+ | |GENE= CNTN2, TAG1, TAX ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
+ | }} | ||
+ | |||
+ | '''N-Terminal Fragment of Human TAX1''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 2OM5 is a [ | + | 2OM5 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OM5 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/17766378 17766378] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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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 Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:01:30 2008'' |
Revision as of 16:01, 20 March 2008
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, resolution 3.07Å | |||||||
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Gene: | CNTN2, TAG1, TAX (Homo sapiens) | ||||||
Coordinates: | save as pdb, mmCIF, xml |
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 Thu Mar 20 18:01:30 2008