1g0y
From Proteopedia
(New page: 200px<br /> <applet load="1g0y" size="450" color="white" frame="true" align="right" spinBox="true" caption="1g0y, resolution 3.0Å" /> '''IL-1 RECEPTOR TYPE 1...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1g0y.gif|left|200px]]<br /> | + | [[Image:1g0y.gif|left|200px]]<br /><applet load="1g0y" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1g0y" size=" | + | |
caption="1g0y, resolution 3.0Å" /> | caption="1g0y, resolution 3.0Å" /> | ||
'''IL-1 RECEPTOR TYPE 1 COMPLEXED WITH ANTAGONIST PEPTIDE AF10847'''<br /> | '''IL-1 RECEPTOR TYPE 1 COMPLEXED WITH ANTAGONIST PEPTIDE AF10847'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Interleukin (IL-1)alpha and IL-1beta are important mediators of | + | Interleukin (IL-1)alpha and IL-1beta are important mediators of inflammation. The binding of IL-1 to interleukin-1 receptor (IL-1R) type 1 is the initial step in IL-1 signal transduction and therefore is a tempting target for anti-inflammatory therapeutics. To advance our understanding of IL-1R1 binding interactions, we have determined the structure of the extracellular domains of IL-1R1 bound to a 21-amino acid IL-1 antagonist peptide at 3.0-A resolution. The antagonist peptide binds to the domain 1/2 junction of the receptor, which is a conserved binding site for IL-1beta and IL-1 receptor antagonist (IL-1ra). This co-crystal structure also reveals that considerable flexibility is present in IL-1R1 because the carboxyl-terminal domain of the receptor is rotated almost 170 degrees relative to the first two domains of the receptor compared with the previously solved IL-1R1.ligand structures. The structure shows an unexpected binding mode for the peptide and may contribute to the design of smaller IL-1R antagonists. |
==Disease== | ==Disease== | ||
| Line 11: | Line 10: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1G0Y 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:// | + | 1G0Y 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=1G0Y OCA]. |
==Reference== | ==Reference== | ||
| Line 17: | Line 16: | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Brandhuber, B | + | [[Category: Brandhuber, B J.]] |
| - | [[Category: Dripps, D | + | [[Category: Dripps, D J.]] |
| - | [[Category: Edwards, C | + | [[Category: Edwards, C K.]] |
| - | [[Category: Vigers, G | + | [[Category: Vigers, G P.A.]] |
[[Category: immunoglobulin]] | [[Category: immunoglobulin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:44:50 2008'' |
Revision as of 10:44, 21 February 2008
|
IL-1 RECEPTOR TYPE 1 COMPLEXED WITH ANTAGONIST PEPTIDE AF10847
Contents |
Overview
Interleukin (IL-1)alpha and IL-1beta are important mediators of inflammation. The binding of IL-1 to interleukin-1 receptor (IL-1R) type 1 is the initial step in IL-1 signal transduction and therefore is a tempting target for anti-inflammatory therapeutics. To advance our understanding of IL-1R1 binding interactions, we have determined the structure of the extracellular domains of IL-1R1 bound to a 21-amino acid IL-1 antagonist peptide at 3.0-A resolution. The antagonist peptide binds to the domain 1/2 junction of the receptor, which is a conserved binding site for IL-1beta and IL-1 receptor antagonist (IL-1ra). This co-crystal structure also reveals that considerable flexibility is present in IL-1R1 because the carboxyl-terminal domain of the receptor is rotated almost 170 degrees relative to the first two domains of the receptor compared with the previously solved IL-1R1.ligand structures. The structure shows an unexpected binding mode for the peptide and may contribute to the design of smaller IL-1R antagonists.
Disease
Known diseases associated with this structure: Mental retardation, X-linked, 21/34 OMIM:[300206]
About this Structure
1G0Y is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
X-ray crystal structure of a small antagonist peptide bound to interleukin-1 receptor type 1., Vigers GP, Dripps DJ, Edwards CK 3rd, Brandhuber BJ, J Biol Chem. 2000 Nov 24;275(47):36927-33. PMID:10903327
Page seeded by OCA on Thu Feb 21 12:44:50 2008
