1irp
From Proteopedia
(New page: 200px<br /> <applet load="1irp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1irp" /> '''SOLUTION STRUCTURE OF HUMAN INTERLEUKIN-1 R...) |
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| - | [[Image:1irp.gif|left|200px]]<br /> | + | [[Image:1irp.gif|left|200px]]<br /><applet load="1irp" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1irp" size=" | + | |
caption="1irp" /> | caption="1irp" /> | ||
'''SOLUTION STRUCTURE OF HUMAN INTERLEUKIN-1 RECEPTOR ANTAGONIST PROTEIN'''<br /> | '''SOLUTION STRUCTURE OF HUMAN INTERLEUKIN-1 RECEPTOR ANTAGONIST PROTEIN'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Interleukin-1 receptor antagonist protein (IRAP) is a naturally occurring | + | Interleukin-1 receptor antagonist protein (IRAP) is a naturally occurring inhibitor of the interleukin-1 receptor. In contrast to IL-1 beta, IRAP binds to the IL-1 receptor but does not elicit a physiological response. We have determined the solution structure of IRAP using NMR spectroscopy. While the overall topology of the two 153-residue proteins is quite similar, functionally critical differences exist concerning the residues of the linear amino acid sequence that constitute structurally homologous regions in the two proteins. Structurally homologous residues important for IL-1 receptor binding are conserved between IRAP and IL-1 beta. By contrast, structurally homologous residues critical for receptor activation are not conserved between the two proteins. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1IRP 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:// | + | 1IRP 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=1IRP OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Scahill, T | + | [[Category: Scahill, T A.]] |
| - | [[Category: Stockman, B | + | [[Category: Stockman, B J.]] |
| - | [[Category: Strakalaitis, N | + | [[Category: Strakalaitis, N A.]] |
[[Category: cytokine]] | [[Category: cytokine]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:14:54 2008'' |
Revision as of 11:14, 21 February 2008
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SOLUTION STRUCTURE OF HUMAN INTERLEUKIN-1 RECEPTOR ANTAGONIST PROTEIN
Contents |
Overview
Interleukin-1 receptor antagonist protein (IRAP) is a naturally occurring inhibitor of the interleukin-1 receptor. In contrast to IL-1 beta, IRAP binds to the IL-1 receptor but does not elicit a physiological response. We have determined the solution structure of IRAP using NMR spectroscopy. While the overall topology of the two 153-residue proteins is quite similar, functionally critical differences exist concerning the residues of the linear amino acid sequence that constitute structurally homologous regions in the two proteins. Structurally homologous residues important for IL-1 receptor binding are conserved between IRAP and IL-1 beta. By contrast, structurally homologous residues critical for receptor activation are not conserved between the two proteins.
Disease
Known diseases associated with this structure: Gastric cancer risk after H. pylori infection OMIM:[147679], Mental retardation, X-linked, 21/34 OMIM:[300206]
About this Structure
1IRP is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Solution structure of human interleukin-1 receptor antagonist protein., Stockman BJ, Scahill TA, Strakalaitis NA, Brunner DP, Yem AW, Deibel MR Jr, FEBS Lett. 1994 Jul 25;349(1):79-83. PMID:8045306
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