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1hzi

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(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...)
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Revision as of 15:18, 12 November 2007

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 SO4 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

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