2fl5: Difference between revisions
New page: left|200px<br /> <applet load="2fl5" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fl5, resolution 3.00Å" /> '''Cofactor-containing... |
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[[Image:2fl5.gif|left|200px]]<br /> | [[Image:2fl5.gif|left|200px]]<br /><applet load="2fl5" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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caption="2fl5, resolution 3.00Å" /> | caption="2fl5, resolution 3.00Å" /> | ||
'''Cofactor-containing antibodies: Crystal structure of the original yellow antibody'''<br /> | '''Cofactor-containing antibodies: Crystal structure of the original yellow antibody'''<br /> | ||
==Overview== | ==Overview== | ||
Antibodies are generally thought to be a class of proteins that function | 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. | ||
==About this Structure== | ==About this Structure== | ||
2FL5 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with RBF as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | 2FL5 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=RBF:'>RBF</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FL5 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Wilson, I | [[Category: Wilson, I A.]] | ||
[[Category: Zhu, X.]] | [[Category: Zhu, X.]] | ||
[[Category: RBF]] | [[Category: RBF]] | ||
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[[Category: riboflavin-binding]] | [[Category: riboflavin-binding]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:22:27 2008'' |
Revision as of 18:22, 21 February 2008
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Cofactor-containing antibodies: Crystal structure of the original yellow antibody
OverviewOverview
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.
About this StructureAbout this Structure
2FL5 is a Protein complex structure of sequences from Homo sapiens with as ligand. 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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