1j0s: Difference between revisions

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[[Image:1j0s.gif|left|200px]]<br />

[[Image:1j0s.gif|left|200px]]<br /><applet load="1j0s" size="350" color="white" frame="true" align="right" spinBox="true"

<applet load="1j0s" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="1j0s" />

'''Solution structure of the human interleukin-18'''<br />

==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.

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 [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].

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==

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[[Category: beta trefoil]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Mon Nov 12~~ 17:~~36:15 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:17:47 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1j0s.gif|left|200px]]<br />
+[[Image:1j0s.gif|left|200px]]<br /><applet load="1j0s" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="1j0s" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1j0s" />
 '''Solution structure of the human interleukin-18'''<br />
 ==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.
+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==
-J0S 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].
+J0S 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==
@@ Line 26: / Line 25: @@
 [[Category: beta trefoil]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:36:15 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:17:47 2008''