1za3

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(New page: 200px<br /> <applet load="1za3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1za3, resolution 3.35&Aring;" /> '''The crystal structu...)
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[[Image:1za3.gif|left|200px]]<br />
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[[Image:1za3.gif|left|200px]]<br /><applet load="1za3" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="1za3" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1za3, resolution 3.35&Aring;" />
caption="1za3, resolution 3.35&Aring;" />
'''The crystal structure of the YSd1 Fab bound to DR5'''<br />
'''The crystal structure of the YSd1 Fab bound to DR5'''<br />
==Overview==
==Overview==
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Functional antibodies were obtained from a library of antigen-binding, sites generated by a binary code restricted to tyrosine and serine. An, antibody raised against human vascular endothelial growth factor, recognized the antigen with high affinity (K(D)=60 nM) and high, specificity in cell-based assays. The crystal structure of another antigen, binding fragment in complex with its antigen (human death receptor DR5), revealed the structural basis for this minimalist mode of molecular, recognition. Natural antigen-binding sites are enriched for tyrosine and, serine, and we show that these amino acid residues are intrinsically well, suited for molecular recognition. Furthermore, these results demonstrate, that molecular recognition can evolve from even the simplest chemical, diversity.
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Functional antibodies were obtained from a library of antigen-binding sites generated by a binary code restricted to tyrosine and serine. An antibody raised against human vascular endothelial growth factor recognized the antigen with high affinity (K(D)=60 nM) and high specificity in cell-based assays. The crystal structure of another antigen binding fragment in complex with its antigen (human death receptor DR5) revealed the structural basis for this minimalist mode of molecular recognition. Natural antigen-binding sites are enriched for tyrosine and serine, and we show that these amino acid residues are intrinsically well suited for molecular recognition. Furthermore, these results demonstrate that molecular recognition can evolve from even the simplest chemical diversity.
==Disease==
==Disease==
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==About this Structure==
==About this Structure==
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1ZA3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ZA3 OCA].
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1ZA3 is a [http://en.wikipedia.org/wiki/Single_protein 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=1ZA3 OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Compaan, D.M.]]
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[[Category: Compaan, D M.]]
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[[Category: Fellouse, F.A.]]
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[[Category: Fellouse, F A.]]
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[[Category: Hymowitz, S.G.]]
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[[Category: Hymowitz, S G.]]
[[Category: Li, B.]]
[[Category: Li, B.]]
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[[Category: Peden, A.A.]]
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[[Category: Peden, A A.]]
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[[Category: Sidhu, S.S.]]
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[[Category: Sidhu, S S.]]
[[Category: antibody library]]
[[Category: antibody library]]
[[Category: combinatorial mutagenesis]]
[[Category: combinatorial mutagenesis]]
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[[Category: protein engineering]]
[[Category: protein engineering]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:31:42 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:13:33 2008''

Revision as of 14:13, 21 February 2008


1za3, resolution 3.35Å

Drag the structure with the mouse to rotate

The crystal structure of the YSd1 Fab bound to DR5

Contents

Overview

Functional antibodies were obtained from a library of antigen-binding sites generated by a binary code restricted to tyrosine and serine. An antibody raised against human vascular endothelial growth factor recognized the antigen with high affinity (K(D)=60 nM) and high specificity in cell-based assays. The crystal structure of another antigen binding fragment in complex with its antigen (human death receptor DR5) revealed the structural basis for this minimalist mode of molecular recognition. Natural antigen-binding sites are enriched for tyrosine and serine, and we show that these amino acid residues are intrinsically well suited for molecular recognition. Furthermore, these results demonstrate that molecular recognition can evolve from even the simplest chemical diversity.

Disease

Known diseases associated with this structure: Squamous cell carcinoma, head and neck OMIM:[603612]

About this Structure

1ZA3 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Molecular recognition by a binary code., Fellouse FA, Li B, Compaan DM, Peden AA, Hymowitz SG, Sidhu SS, J Mol Biol. 2005 May 20;348(5):1153-62. Epub 2005 Apr 1. PMID:15854651

Page seeded by OCA on Thu Feb 21 16:13:33 2008

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