1iar

From Proteopedia

(Difference between revisions)

Current revision

INTERLEUKIN-4 / RECEPTOR ALPHA CHAIN COMPLEX

Structural highlights

1iar is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.3Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

IL4RA_HUMAN Receptor for both interleukin 4 and interleukin 13. Couples to the JAK1/2/3-STAT6 pathway. The IL4 response is involved in promoting Th2 differentiation. The IL4/IL13 responses are involved in regulating IgE production and, chemokine and mucus production at sites of allergic inflammation. In certain cell types, can signal through activation of insulin receptor substrates, IRS1/IRS2.^[1] Soluble IL4R (sIL4R) inhibits IL4-mediated cell proliferation and IL5 up-regulation by T-cells.^[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Interleukin-4 (IL-4) is a principal regulatory cytokine during an immune response and a crucial determinant for allergy and asthma. IL-4 binds with high affinity and specificity to the ectodomain of the IL-4 receptor alpha chain (IL4-BP). Subsequently, this intermediate complex recruits the common gamma chain (gamma c), thereby initiating transmembrane signaling. The crystal structure of the intermediate complex between human IL-4 and IL4-BP was determined at 2.3 A resolution. It reveals a novel spatial orientation of the two proteins, a small but unexpected conformational change in the receptor-bound IL-4, and an interface with three separate clusters of trans-interacting residues. Novel insights on ligand binding in the cytokine receptor family and a paradigm for receptors of IL-2, IL-7, IL-9, and IL-15, which all utilize gamma c, are provided.

Crystal structure of the interleukin-4/receptor alpha chain complex reveals a mosaic binding interface.,Hage T, Sebald W, Reinemer P Cell. 1999 Apr 16;97(2):271-81. PMID:10219247^[3]

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

References

↑ Keegan AD, Nelms K, White M, Wang LM, Pierce JH, Paul WE. An IL-4 receptor region containing an insulin receptor motif is important for IL-4-mediated IRS-1 phosphorylation and cell growth. Cell. 1994 Mar 11;76(5):811-20. PMID:8124718
↑ Keegan AD, Nelms K, White M, Wang LM, Pierce JH, Paul WE. An IL-4 receptor region containing an insulin receptor motif is important for IL-4-mediated IRS-1 phosphorylation and cell growth. Cell. 1994 Mar 11;76(5):811-20. PMID:8124718
↑ Hage T, Sebald W, Reinemer P. Crystal structure of the interleukin-4/receptor alpha chain complex reveals a mosaic binding interface. Cell. 1999 Apr 16;97(2):271-81. PMID:10219247

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1iar"

Categories: Homo sapiens | Large Structures | Hage T | Reinemer P | Sebald W

@@ Line 1: / Line 1: @@
-[[Image:1iar.gif|left|200px]]<br />
-<applet load="1iar" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1iar, resolution 2.3&Aring;" />
-'''INTERLEUKIN-4 / RECEPTOR ALPHA CHAIN COMPLEX'''<br />
-==Overview==
+==INTERLEUKIN-4 / RECEPTOR ALPHA CHAIN COMPLEX==
-Interleukin-4 (IL-4) is a principal regulatory cytokine during an immune, response and a crucial determinant for allergy and asthma. IL-4 binds with, high affinity and specificity to the ectodomain of the IL-4 receptor alpha, chain (IL4-BP). Subsequently, this intermediate complex recruits the, common gamma chain (gamma c), thereby initiating transmembrane signaling., The crystal structure of the intermediate complex between human IL-4 and, IL4-BP was determined at 2.3 A resolution. It reveals a novel spatial, orientation of the two proteins, a small but unexpected conformational, change in the receptor-bound IL-4, and an interface with three separate, clusters of trans-interacting residues. Novel insights on ligand binding, in the cytokine receptor family and a paradigm for receptors of IL-2, IL-7, IL-9, and IL-15, which all utilize gamma c, are provided.
+<StructureSection load='1iar' size='340' side='right'caption='[[1iar]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1iar]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IAR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IAR FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1iar FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iar OCA], [https://pdbe.org/1iar PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1iar RCSB], [https://www.ebi.ac.uk/pdbsum/1iar PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1iar ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/IL4RA_HUMAN IL4RA_HUMAN] Receptor for both interleukin 4 and interleukin 13. Couples to the JAK1/2/3-STAT6 pathway. The IL4 response is involved in promoting Th2 differentiation. The IL4/IL13 responses are involved in regulating IgE production and, chemokine and mucus production at sites of allergic inflammation. In certain cell types, can signal through activation of insulin receptor substrates, IRS1/IRS2.<ref>PMID:8124718</ref>   Soluble IL4R (sIL4R) inhibits IL4-mediated cell proliferation and IL5 up-regulation by T-cells.<ref>PMID:8124718</ref>
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ia/1iar_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1iar ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Interleukin-4 (IL-4) is a principal regulatory cytokine during an immune response and a crucial determinant for allergy and asthma. IL-4 binds with high affinity and specificity to the ectodomain of the IL-4 receptor alpha chain (IL4-BP). Subsequently, this intermediate complex recruits the common gamma chain (gamma c), thereby initiating transmembrane signaling. The crystal structure of the intermediate complex between human IL-4 and IL4-BP was determined at 2.3 A resolution. It reveals a novel spatial orientation of the two proteins, a small but unexpected conformational change in the receptor-bound IL-4, and an interface with three separate clusters of trans-interacting residues. Novel insights on ligand binding in the cytokine receptor family and a paradigm for receptors of IL-2, IL-7, IL-9, and IL-15, which all utilize gamma c, are provided.
-==Disease==
+Crystal structure of the interleukin-4/receptor alpha chain complex reveals a mosaic binding interface.,Hage T, Sebald W, Reinemer P Cell. 1999 Apr 16;97(2):271-81. PMID:10219247<ref>PMID:10219247</ref>
-Known diseases associated with this structure: AIDS, slow progression to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=147781 147781]], Atopy, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=147781 147781]]
-==About this Structure==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-IAR is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences 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=1IAR OCA].
+</div>
+<div class="pdbe-citations 1iar" style="background-color:#fffaf0;"></div>
-==Reference==
+==See Also==
-Crystal structure of the interleukin-4/receptor alpha chain complex reveals a mosaic binding interface., Hage T, Sebald W, Reinemer P, Cell. 1999 Apr 16;97(2):271-81. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10219247 10219247]
+*[[Interleukin 3D structures|Interleukin 3D structures]]
+*[[Interleukin receptor 3D structures|Interleukin receptor 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Protein complex]]
+[[Category: Large Structures]]
-[[Category: Hage, T.]]
+[[Category: Hage T]]
-[[Category: Reinemer, P.]]
+[[Category: Reinemer P]]
-[[Category: Sebald, W.]]
+[[Category: Sebald W]]
-[[Category: cytokine receptor]]
-[[Category: interleukin-4]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:28:12 2007''

1iar

From Proteopedia

Current revision

INTERLEUKIN-4 / RECEPTOR ALPHA CHAIN COMPLEX

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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