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1oax

From Proteopedia

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[[Image:1oax.jpg|left|200px]]
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{{Seed}}
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{{STRUCTURE_1oax| PDB=1oax | SCENE= }}
{{STRUCTURE_1oax| PDB=1oax | SCENE= }}
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'''FV STRUCTURE OF THE IGE SPE-7 IN COMPLEX WITH ACENAPHTHENEQUINONE'''
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===FV STRUCTURE OF THE IGE SPE-7 IN COMPLEX WITH ACENAPHTHENEQUINONE===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 12610298 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12610298}}
==About this Structure==
==About this Structure==
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[[Category: Antibody]]
[[Category: Antibody]]
[[Category: Ige]]
[[Category: Ige]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:36:47 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 08:12:16 2008''

Revision as of 05:12, 28 July 2008

Image:1oax.png

Template:STRUCTURE 1oax

FV STRUCTURE OF THE IGE SPE-7 IN COMPLEX WITH ACENAPHTHENEQUINONE

Template:ABSTRACT PUBMED 12610298

About this Structure

Full crystallographic information is available from OCA.

Reference

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

Page seeded by OCA on Mon Jul 28 08:12:16 2008

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