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New page: left|200px<br /><applet load="1ver" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ver, resolution 2.82Å" /> '''Structure of New Ant...
 
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[[Image:1ver.jpg|left|200px]]<br /><applet load="1ver" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1ver.jpg|left|200px]]<br /><applet load="1ver" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1ver, resolution 2.82&Aring;" />
caption="1ver, resolution 2.82&Aring;" />
'''Structure of New Antigen Receptor variable domain from sharks'''<br />
'''Structure of New Antigen Receptor variable domain from sharks'''<br />


==Overview==
==Overview==
The Ig new antigen receptors (IgNARs) are single-domain antibodies found, in the serum of sharks. Here, we report 2.2- and 2.8-A structures of the, type 2 IgNAR variable domains 12Y-1 and 12Y-2. Structural features, include, first, an Ig superfamily topology transitional between cell, adhesion molecules, antibodies, and T cell receptors; and, second, a, vestigial complementarity-determining region 2 at the "bottom" of the, molecule, apparently discontinuous from the antigen-binding paratope and, similar to that observed in cell adhesion molecules. Thus, we suggest that, IgNARs originated as cell-surface adhesion molecules coopted to the immune, repertoire and represent an evolutionary lineage independent of variable, heavy chain/variable light chain type antibodies. Additionally, both 12Y-1, and 12Y-2 form unique crystallographic dimers, predominantly mediated by, main-chain framework interactions, which represent a possible model for, primordial cell-based interactions. Unusually, the 12Y-2, complementarity-determining region 3 also adopts an extended beta-hairpin, structure, suggesting a distinct selective advantage in accessing cryptic, antigenic epitopes.
The Ig new antigen receptors (IgNARs) are single-domain antibodies found in the serum of sharks. Here, we report 2.2- and 2.8-A structures of the type 2 IgNAR variable domains 12Y-1 and 12Y-2. Structural features include, first, an Ig superfamily topology transitional between cell adhesion molecules, antibodies, and T cell receptors; and, second, a vestigial complementarity-determining region 2 at the "bottom" of the molecule, apparently discontinuous from the antigen-binding paratope and similar to that observed in cell adhesion molecules. Thus, we suggest that IgNARs originated as cell-surface adhesion molecules coopted to the immune repertoire and represent an evolutionary lineage independent of variable heavy chain/variable light chain type antibodies. Additionally, both 12Y-1 and 12Y-2 form unique crystallographic dimers, predominantly mediated by main-chain framework interactions, which represent a possible model for primordial cell-based interactions. Unusually, the 12Y-2 complementarity-determining region 3 also adopts an extended beta-hairpin structure, suggesting a distinct selective advantage in accessing cryptic antigenic epitopes.


==About this Structure==
==About this Structure==
1VER is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Orectolobus_maculatus Orectolobus maculatus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1VER OCA].  
1VER is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Orectolobus_maculatus Orectolobus maculatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VER OCA].  


==Reference==
==Reference==
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[[Category: Orectolobus maculatus]]
[[Category: Orectolobus maculatus]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Streltsov, V.A.]]
[[Category: Streltsov, V A.]]
[[Category: 12y-1]]
[[Category: 12y-1]]
[[Category: ig vnar]]
[[Category: ig vnar]]
[[Category: native]]
[[Category: native]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 22:18:15 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:34:34 2008''