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.


1hzi

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /> <applet load="1hzi" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hzi, resolution 2.05&Aring;" /> '''INTERLEUKIN-4 MUTAN...)
Line 1: Line 1:
-
[[Image:1hzi.gif|left|200px]]<br />
+
[[Image:1hzi.gif|left|200px]]<br /><applet load="1hzi" size="350" color="white" frame="true" align="right" spinBox="true"
-
<applet load="1hzi" size="450" color="white" frame="true" align="right" spinBox="true"
+
caption="1hzi, resolution 2.05&Aring;" />
caption="1hzi, resolution 2.05&Aring;" />
'''INTERLEUKIN-4 MUTANT E9A'''<br />
'''INTERLEUKIN-4 MUTANT E9A'''<br />
==Overview==
==Overview==
-
Interleukin 4 (IL-4) is a pleiotropic cytokine which induces T-cell, differentiation and class switching of B cells. It therefore plays a, central role in the development of allergies and asthma. An IL-4 variant, in which Glu9 was mutated to alanine shows an 800-fold drop in binding, affinity towards its high-affinity receptor chain. As shown by surface, plasmon resonance measurements, this mostly arises from a decreased, association rate. Here, the crystal structure of this mutant is reported., It reveals that the protein has a virtually identical structure to the, wild type, showing that the unusual behaviour of the mutated protein is, not a consequence of misfolding. The possibility that polar interactions, in the encounter complex have a steering effect is discussed.
+
Interleukin 4 (IL-4) is a pleiotropic cytokine which induces T-cell differentiation and class switching of B cells. It therefore plays a central role in the development of allergies and asthma. An IL-4 variant in which Glu9 was mutated to alanine shows an 800-fold drop in binding affinity towards its high-affinity receptor chain. As shown by surface plasmon resonance measurements, this mostly arises from a decreased association rate. Here, the crystal structure of this mutant is reported. It reveals that the protein has a virtually identical structure to the wild type, showing that the unusual behaviour of the mutated protein is not a consequence of misfolding. The possibility that polar interactions in the encounter complex have a steering effect is discussed.
==Disease==
==Disease==
Line 11: Line 10:
==About this Structure==
==About this Structure==
-
1HZI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HZI OCA].
+
1HZI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HZI OCA].
==Reference==
==Reference==
Line 17: Line 16:
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
-
[[Category: Dreyer, M.K.]]
+
[[Category: Dreyer, M K.]]
[[Category: Hulsmeyer, M.]]
[[Category: Hulsmeyer, M.]]
[[Category: Scheufler, C.]]
[[Category: Scheufler, C.]]
Line 25: Line 24:
[[Category: il-4]]
[[Category: il-4]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:24:35 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:06:22 2008''

Revision as of 11:06, 21 February 2008

Image:1hzi.gif

1hzi, resolution 2.05Å

Drag the structure with the mouse to rotate

INTERLEUKIN-4 MUTANT E9A

Contents

Overview

Interleukin 4 (IL-4) is a pleiotropic cytokine which induces T-cell differentiation and class switching of B cells. It therefore plays a central role in the development of allergies and asthma. An IL-4 variant in which Glu9 was mutated to alanine shows an 800-fold drop in binding affinity towards its high-affinity receptor chain. As shown by surface plasmon resonance measurements, this mostly arises from a decreased association rate. Here, the crystal structure of this mutant is reported. It reveals that the protein has a virtually identical structure to the wild type, showing that the unusual behaviour of the mutated protein is not a consequence of misfolding. The possibility that polar interactions in the encounter complex have a steering effect is discussed.

Disease

Known diseases associated with this structure: AIDS, slow progression to OMIM:[147781], Atopy, susceptibility to OMIM:[147781]

About this Structure

1HZI is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.

Reference

Structure of interleukin 4 mutant E9A suggests polar steering in receptor-complex formation., Hulsmeyer M, Scheufler C, Dreyer MK, Acta Crystallogr D Biol Crystallogr. 2001 Sep;57(Pt 9):1334-6. Epub 2001, Aug 23. PMID:11526337

Page seeded by OCA on Thu Feb 21 13:06:22 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1hzi"
Personal tools