2fl5: Difference between revisions

Revision as of 11:41, 28 July 2008

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File:2fl5.png

Template:STRUCTURE 2fl5

Cofactor-containing antibodies: Crystal structure of the original yellow antibodyCofactor-containing antibodies: Crystal structure of the original yellow antibody

Template:ABSTRACT PUBMED 16537445

About this StructureAbout this Structure

Full crystallographic information is available from OCA.

ReferenceReference

Cofactor-containing antibodies: crystal structure of the original yellow antibody., Zhu X, Wentworth P Jr, Kyle RA, Lerner RA, Wilson IA, Proc Natl Acad Sci U S A. 2006 Mar 7;103(10):3581-5. Epub 2006 Feb 28. PMID:16537445

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Cofactor-containing antibodies: Crystal structure of the original yellow antibody'''
+===Cofactor-containing antibodies: Crystal structure of the original yellow antibody===
-==Overview==
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-Antibodies are generally thought to be a class of proteins that function without the use of cofactors. However, it is not widely appreciated that antibodies are believed to be the major carrier protein in human circulation for the important riboflavin cofactor that is involved in a host of biological phenomena. A further link between riboflavin and antibodies was discovered 30 years ago when a bright-yellow antibody, IgG(GAR), was purified from a patient with multiple myeloma who had turned yellow during the course of her disease. It was subsequently shown that the yellow color of this antibody was due to riboflavin binding. However, it was not known how and where riboflavin was bound to this antibody. We now report the crystal structure of this historically important IgG(GAR) Fab at 3.0-A resolution. The riboflavin is located in the antigen-combining site with its isoalloxazine ring stacked between the parallel aromatic moieties of TyrH33, PheH58, and TyrH100A. Together with additional hydrogen bonds, these interactions reveal the structural basis for high-affinity riboflavin binding. The ligand specificity of IgG(GAR) is compared with another riboflavin-binding antibody, IgG(DOT), which was purified from a second patient with multiple myeloma. The crystal structure of IgG(GAR) provides a starting point for attempts to understand the physiological relevance and chemical functions of cofactor-containing antibodies.
+The line below this paragraph, {{ABSTRACT_PUBMED_16537445}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_16537445}}
 ==About this Structure==
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 [[Category: Multiple myeloma]]
 [[Category: Riboflavin-binding]]
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