1j0s

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(New page: 200px<br /> <applet load="1j0s" size="450" color="white" frame="true" align="right" spinBox="true" caption="1j0s" /> '''Solution structure of the human interleukin...)
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'''Solution structure of the human interleukin-18'''<br />
'''Solution structure of the human interleukin-18'''<br />
==Overview==
==Overview==
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Interleukin-18 (IL-18), a cytokine formerly known as interferon-gamma-, (IFN-gamma-) inducing factor, has pleiotropic immunoregulatory functions, including augmentation of IFN-gamma production, Fas-mediated cytotoxicity, and developmental regulation of T-lymphocyte helper type I. We determined, the solution structure of IL-18 as a first step toward understanding its, receptor activation mechanism. It folds into a beta-trefoil structure that, resembles that of IL-1. Extensive mutagenesis revealed the presence of, three sites that are important for receptor activation: two serve as, binding sites for IL-18 receptor alpha (IL-18Ralpha), located at positions, similar to those of IL-1 for IL-1 receptor type I (IL-1RI), whereas the, third site may be involved in IL-18 receptor beta (IL-18Rbeta) binding., The structure and mutagenesis data provide a basis for understanding the, IL-18-induced heterodimerization of receptor subunits, which is necessary, for receptor activation.
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Interleukin-18 (IL-18), a cytokine formerly known as interferon-gamma- (IFN-gamma-) inducing factor, has pleiotropic immunoregulatory functions, including augmentation of IFN-gamma production, Fas-mediated cytotoxicity and developmental regulation of T-lymphocyte helper type I. We determined the solution structure of IL-18 as a first step toward understanding its receptor activation mechanism. It folds into a beta-trefoil structure that resembles that of IL-1. Extensive mutagenesis revealed the presence of three sites that are important for receptor activation: two serve as binding sites for IL-18 receptor alpha (IL-18Ralpha), located at positions similar to those of IL-1 for IL-1 receptor type I (IL-1RI), whereas the third site may be involved in IL-18 receptor beta (IL-18Rbeta) binding. The structure and mutagenesis data provide a basis for understanding the IL-18-induced heterodimerization of receptor subunits, which is necessary for receptor activation.
==About this Structure==
==About this Structure==
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1J0S 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=1J0S OCA].
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1J0S 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=1J0S OCA].
==Reference==
==Reference==
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[[Category: beta trefoil]]
[[Category: beta trefoil]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:36:15 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:17:47 2008''

Revision as of 11:17, 21 February 2008

Image:1j0s.gif

1j0s

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Solution structure of the human interleukin-18

Overview

Interleukin-18 (IL-18), a cytokine formerly known as interferon-gamma- (IFN-gamma-) inducing factor, has pleiotropic immunoregulatory functions, including augmentation of IFN-gamma production, Fas-mediated cytotoxicity and developmental regulation of T-lymphocyte helper type I. We determined the solution structure of IL-18 as a first step toward understanding its receptor activation mechanism. It folds into a beta-trefoil structure that resembles that of IL-1. Extensive mutagenesis revealed the presence of three sites that are important for receptor activation: two serve as binding sites for IL-18 receptor alpha (IL-18Ralpha), located at positions similar to those of IL-1 for IL-1 receptor type I (IL-1RI), whereas the third site may be involved in IL-18 receptor beta (IL-18Rbeta) binding. The structure and mutagenesis data provide a basis for understanding the IL-18-induced heterodimerization of receptor subunits, which is necessary for receptor activation.

About this Structure

1J0S is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

The structure and binding mode of interleukin-18., Kato Z, Jee J, Shikano H, Mishima M, Ohki I, Ohnishi H, Li A, Hashimoto K, Matsukuma E, Omoya K, Yamamoto Y, Yoneda T, Hara T, Kondo N, Shirakawa M, Nat Struct Biol. 2003 Nov;10(11):966-71. Epub 2003 Oct 5. PMID:14528293

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