This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1g0y

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /> <applet load="1g0y" size="450" color="white" frame="true" align="right" spinBox="true" caption="1g0y, resolution 3.0&Aring;" /> '''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="450" color="white" frame="true" align="right" spinBox="true"
+
caption="1g0y, resolution 3.0&Aring;" />
caption="1g0y, resolution 3.0&Aring;" />
'''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, 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.
+
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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1G0Y OCA].
+
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.J.]]
+
[[Category: Brandhuber, B J.]]
-
[[Category: Dripps, D.J.]]
+
[[Category: Dripps, D J.]]
-
[[Category: Edwards, C.K.]]
+
[[Category: Edwards, C K.]]
-
[[Category: Vigers, G.P.A.]]
+
[[Category: Vigers, G P.A.]]
[[Category: immunoglobulin]]
[[Category: immunoglobulin]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:59:11 2007''
+
''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


1g0y, resolution 3.0Å

Drag the structure with the mouse to rotate

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools