1CYL

ASPECTS OF RECEPTOR BINDING AND SIGNALLING OF INTERLEUKIN-4 INVESTIGATED BY SITE-DIRECTED MUTAGENESIS AND NMR SPECTROSCOPY


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Submitted: 20 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Aspects of receptor binding and signalling of interleukin-4 investigated by site-directed mutagenesis and NMR spectroscopy.

Muller, T.Dieckmann, T.Sebald, W.Oschkinat, H.

(1994) J Mol Biol 237: 423-436

  • DOI: https://doi.org/10.1006/jmbi.1994.1245
  • Primary Citation of Related Structures:  
    1CYL, 2CYK

  • PubMed Abstract: 

    Cytokines are hormones that carry information from cell to cell. This information is read from their surface upon binding to transmembrane receptors and by the subsequent initiation of receptor oligomerization. An influence on this process through mutagenesis on the hormone surface is highly desirable for medical reasons. However, an understanding of hormone-receptor interactions requires insight into the structural changes introduced by the mutations. In this line structural studies on human IL-4 and the medically important IL-4 antagonists Y124D and Y124G are presented. The site around Y124 is an important epitope responsible for the ability of IL-4 to cause a signal in the target cells. It is shown that the local main-chain structure around residue 124 in the variants remains unchanged. A strategy is presented here which allows the study of these types of proteins and their variants by NMR which does not require carbon labelled samples.


  • Organizational Affiliation

    Theodor-Boveri-Institut für Biowissenschaften (Biozentrum) Universität Würzburg, Germany.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
INTERLEUKIN-4129Homo sapiensMutation(s): 0 
UniProt & NIH Common Fund Data Resources
Find proteins for P05112 (Homo sapiens)
Explore P05112 
Go to UniProtKB:  P05112
PHAROS:  P05112
GTEx:  ENSG00000113520 
Entity Groups  
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UniProt GroupP05112
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Submitted: 20 

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1994-09-30
    Type: Initial release
  • Version 1.1: 2008-03-24
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2022-02-16
    Changes: Database references, Derived calculations, Other