1iar
From Proteopedia
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[[Image:1iar.jpg|left|200px]] | [[Image:1iar.jpg|left|200px]] | ||
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'''INTERLEUKIN-4 / RECEPTOR ALPHA CHAIN COMPLEX''' | '''INTERLEUKIN-4 / RECEPTOR ALPHA CHAIN COMPLEX''' | ||
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[[Category: Reinemer, P.]] | [[Category: Reinemer, P.]] | ||
[[Category: Sebald, W.]] | [[Category: Sebald, W.]] | ||
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Revision as of 16:46, 2 May 2008
INTERLEUKIN-4 / RECEPTOR ALPHA CHAIN COMPLEX
Overview
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.
About this Structure
1IAR is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Fri May 2 19:46:54 2008
