1ilt: Difference between revisions

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

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

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

caption="1ilt, resolution 2.0Å" />

'''X-RAY STRUCTURE OF INTERLEUKIN-1 RECEPTOR ANTAGONIST AT 2.0 ANGSTROMS RESOLUTION'''<br />

==Overview==

Interleukin-1 receptor antagonist (IL-1ra) is a natural competitive, antagonist of IL-1. In order to further elucidate the mechanism by which, IL-1ra binds without activating the IL-1 receptor, we have solved the, crystal structure of IL-1ra at 2.0-A resolution. IL-1ra has the same, overall beta-trefoil fold as IL-1 alpha and IL-1 beta and has a very, similar hydrophobic core. However, there are a number of structural, differences between the molecules, including significant differences at, the open end of the beta-barrel, which has been identified in IL-1 beta as, a receptor binding site.

Interleukin-1 receptor antagonist (IL-1ra) is a natural competitive antagonist of IL-1. In order to further elucidate the mechanism by which IL-1ra binds without activating the IL-1 receptor, we have solved the crystal structure of IL-1ra at 2.0-A resolution. IL-1ra has the same overall beta-trefoil fold as IL-1 alpha and IL-1 beta and has a very similar hydrophobic core. However, there are a number of structural differences between the molecules, including significant differences at the open end of the beta-barrel, which has been identified in IL-1 beta as a receptor binding site.

==Disease==

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==About this Structure==

1ILT 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=1ILT OCA].

1ILT 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=1ILT OCA].

==Reference==

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[[Category: Homo sapiens]]

[[Category: Single protein]]

[[Category: Brandhuber, B.J.]]

[[Category: Brandhuber, B J.]]

[[Category: Vigers, G.P.A.]]

[[Category: Vigers, G P.A.]]

[[Category: cytokine]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Mon Nov 12 17~~:31:~~27 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:13:10 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1ilt.gif|left|200px]]<br />
+[[Image:1ilt.gif|left|200px]]<br /><applet load="1ilt" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="1ilt" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1ilt, resolution 2.0&Aring;" />
 '''X-RAY STRUCTURE OF INTERLEUKIN-1 RECEPTOR ANTAGONIST AT 2.0 ANGSTROMS RESOLUTION'''<br />
 ==Overview==
-Interleukin-1 receptor antagonist (IL-1ra) is a natural competitive, antagonist of IL-1. In order to further elucidate the mechanism by which, IL-1ra binds without activating the IL-1 receptor, we have solved the, crystal structure of IL-1ra at 2.0-A resolution. IL-1ra has the same, overall beta-trefoil fold as IL-1 alpha and IL-1 beta and has a very, similar hydrophobic core. However, there are a number of structural, differences between the molecules, including significant differences at, the open end of the beta-barrel, which has been identified in IL-1 beta as, a receptor binding site.
+Interleukin-1 receptor antagonist (IL-1ra) is a natural competitive antagonist of IL-1. In order to further elucidate the mechanism by which IL-1ra binds without activating the IL-1 receptor, we have solved the crystal structure of IL-1ra at 2.0-A resolution. IL-1ra has the same overall beta-trefoil fold as IL-1 alpha and IL-1 beta and has a very similar hydrophobic core. However, there are a number of structural differences between the molecules, including significant differences at the open end of the beta-barrel, which has been identified in IL-1 beta as a receptor binding site.
 ==Disease==
@@ Line 11: / Line 10: @@
 ==About this Structure==
-ILT 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=1ILT OCA].
+ILT 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=1ILT OCA].
 ==Reference==
@@ Line 17: / Line 16: @@
 [[Category: Homo sapiens]]
 [[Category: Single protein]]
-[[Category: Brandhuber, B.J.]]
+[[Category: Brandhuber, B J.]]
-[[Category: Vigers, G.P.A.]]
+[[Category: Vigers, G P.A.]]
 [[Category: cytokine]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:31:27 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:13:10 2008''