1oay: Difference between revisions

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[[Image:1oay.jpg|left|200px]]<br /><applet load="1oay" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1oay.jpg|left|200px]]<br /><applet load="1oay" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1oay, resolution 2.66&Aring;" />
caption="1oay, resolution 2.66&Aring;" />
'''ANTIBODY MULTISPECIFICITY MEDIATED BY CONFORMATIONAL DIVERSITY'''<br />
'''ANTIBODY MULTISPECIFICITY MEDIATED BY CONFORMATIONAL DIVERSITY'''<br />
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==About this Structure==
==About this Structure==
1OAY is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_rattus Rattus rattus] with FUR as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=AC1:Fur Binding Site For Chain J'>AC1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OAY OCA].  
1OAY is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_rattus Rattus rattus] with <scene name='pdbligand=FUR:'>FUR</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=AC1:Fur+Binding+Site+For+Chain+J'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OAY OCA].  


==Reference==
==Reference==
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[[Category: multispecificity]]
[[Category: multispecificity]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 17:17:38 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 09:55:43 2008''

Revision as of 10:55, 3 February 2008

File:1oay.jpg


1oay, resolution 2.66Å

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ANTIBODY MULTISPECIFICITY MEDIATED BY CONFORMATIONAL DIVERSITY

OverviewOverview

A single antibody was shown to adopt different binding-site conformations, and thereby bind unrelated antigens. Analysis by both x-ray, crystallography and pre-steady-state kinetics revealed an equilibrium, between different preexisting isomers, one of which possessed a, promiscuous, low-affinity binding site for aromatic ligands, including the, immunizing hapten. A subsequent induced-fit isomerization led to, high-affinity complexes with a deep and narrow binding site. A protein, antigen identified by repertoire selection made use of an unrelated, antibody isomer with a wide, shallow binding site. Conformational, diversity, whereby one sequence adopts multiple structures and multiple, functions, can increase the effective size of the antibody repertoire but, may also lead to autoimmunity and allergy.

About this StructureAbout this Structure

1OAY is a Protein complex structure of sequences from Rattus rattus with as ligand. Known structural/functional Site: . Full crystallographic information is available from OCA.

ReferenceReference

Antibody multispecificity mediated by conformational diversity., James LC, Roversi P, Tawfik DS, Science. 2003 Feb 28;299(5611):1362-7. PMID:12610298

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