View source for 2om5


==N-Terminal Fragment of Human TAX1==
<StructureSection load='2om5' size='340' side='right'caption='[[2om5]], [[Resolution|resolution]] 3.07&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2om5]] is a 1 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OM5 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.07&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2om5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2om5 OCA], [https://pdbe.org/2om5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2om5 RCSB], [https://www.ebi.ac.uk/pdbsum/2om5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2om5 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CNTN2_HUMAN CNTN2_HUMAN] May play a role in the initial growth and guidance of axons. May be involved in cell adhesion.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/om/2om5_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2om5 ConSurf].
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== Publication Abstract from PubMed ==
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 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<ref>PMID:17766378</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Diederichs K]]
[[Category: Moertl M]]
[[Category: Sonderegger P]]
[[Category: Welte W]]