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1cyl

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1cyl, 20 NMR models ()

Domains:

IL4

Related:

2cyk

Structural annotation:
Resources:	CATH : 1Cyl000 InterPro : Ipr002354, Ipr012351, Ipr009079, Ipr001325 Pfam : PF00727 SCOP : d1cyl__ UniProt : P05112

Functional annotation:
Resources:	GeneCard : IL4
Cellular component:	extracellular region extracellular space
Biological process:	regulation of isotype switching positive regulation of MHC class II biosynthetic process connective tissue growth factor biosynthetic process B cell differentiation chemotaxis positive regulation of isotype switching to IgG isotypes positive regulation of isotype switching to IgE isotypes T-helper 2 type immune response B cell activation positive regulation of T cell proliferation cholesterol metabolic process positive regulation of transcription from RNA polymerase II promoter negative regulation of osteoclast differentiation cellular defense response regulation of immune response regulation of phosphorylation negative regulation of apoptosis immune response positive regulation of B cell proliferation
Molecular function:	hematopoietin/interferon-class (D200-domain) cytokine receptor binding protein binding cytokine activity growth factor activity interleukin-4 receptor binding

Evolutionary conservation:

Toggle Conservation Colors:	Rows = identical sequences:
Further Information:	Caveats, Explanation, Complete Results at ConSurfDB

Resources:

FirstGlance, OCA, PDBsum, RCSB

Coordinates:

save as pdb, mmCIF, xml

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

Publication Abstract from PubMed

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.

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, J Mol Biol. 1994 Apr 8;237(4):423-36. PMID:8151703

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

1CYL is a 1 chain structure of sequence from Homo sapiens. Full experimental information is available from OCA.

Reference

Muller T, Dieckmann T, Sebald W, Oschkinat H. Aspects of receptor binding and signalling of interleukin-4 investigated by site-directed mutagenesis and NMR spectroscopy. J Mol Biol. 1994 Apr 8;237(4):423-36. PMID:8151703

Page seeded by OCA on Mon Feb 16 21:47:44 2009