1ves
From Proteopedia
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| - | [[Image:1ves.jpg|left|200px]] | + | [[Image:1ves.jpg|left|200px]] |
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| - | '''Structure of New Antigen Receptor variable domain from sharks''' | + | {{Structure |
| + | |PDB= 1ves |SIZE=350|CAPTION= <scene name='initialview01'>1ves</scene>, resolution 2.18Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''Structure of New Antigen Receptor variable domain from sharks''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1VES is a [ | + | 1VES is a [[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=1VES OCA]. |
==Reference== | ==Reference== | ||
| - | Structural evidence for evolution of shark Ig new antigen receptor variable domain antibodies from a cell-surface receptor., Streltsov VA, Varghese JN, Carmichael JA, Irving RA, Hudson PJ, Nuttall SD, Proc Natl Acad Sci U S A. 2004 Aug 24;101(34):12444-9. Epub 2004 Aug 10. PMID:[http:// | + | Structural evidence for evolution of shark Ig new antigen receptor variable domain antibodies from a cell-surface receptor., Streltsov VA, Varghese JN, Carmichael JA, Irving RA, Hudson PJ, Nuttall SD, Proc Natl Acad Sci U S A. 2004 Aug 24;101(34):12444-9. Epub 2004 Aug 10. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15304650 15304650] |
[[Category: Orectolobus maculatus]] | [[Category: Orectolobus maculatus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: ig vnar]] | [[Category: ig vnar]] | ||
| - | ''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 14:44:34 2008'' |
Revision as of 12:44, 20 March 2008
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Structure of New Antigen Receptor variable domain from sharks
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.
About this Structure
1VES is a Single protein structure of sequence from Orectolobus maculatus. Full crystallographic information is available from OCA.
Reference
Structural evidence for evolution of shark Ig new antigen receptor variable domain antibodies from a cell-surface receptor., Streltsov VA, Varghese JN, Carmichael JA, Irving RA, Hudson PJ, Nuttall SD, Proc Natl Acad Sci U S A. 2004 Aug 24;101(34):12444-9. Epub 2004 Aug 10. PMID:15304650
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