2B90

Crystal structure of the interleukin-4 variant T13DR85A

Summary for 2B90

• Entry DOI: 10.2210/pdb2b90/pdb
• Related: 2B8U 2B8X 2B8Y 2B8Z 2B91 2D48
• Descriptor: Interleukin-4, SULFATE ION (3 entities in total)
• Functional Keywords: four helix bundle, cytokine
• Biological source: Homo sapiens (human)
• Cellular location: Secreted: P05112
• Total number of polymer chains: 1
• Total formula weight: 15205.30

Authors

Kraich, M.,Klein, M.,Patino, E.,Harrer, H.,Sebald, W.,Mueller, T.D. (deposition date: 2005-10-10, release date: 2006-05-30, Last modification date: 2024-10-23)

Primary citation

Kraich, M.,Klein, M.,Patino, E.,Harrer, H.,Nickel, J.,Sebald, W.,Mueller, T.D.
A modular interface of IL-4 allows for scalable affinity without affecting specificity for the IL-4 receptor
Bmc Biol., 4:13-13, 2006

PubMed Abstract: Interleukin 4 (IL-4) is a key regulator of the immune system and an important factor in the development of allergic hypersensitivity. Together with interleukin 13 (IL-13), IL-4 plays an important role in exacerbating allergic and asthmatic symptoms. For signal transduction, both cytokines can utilise the same receptor, consisting of the IL-4Ralpha and the IL-13Ralpha1 chain, offering an explanation for their overlapping biological functions. Since both cytokine ligands share only moderate similarity on the amino acid sequence level, molecular recognition of the ligands by both receptor subunits is of great interest. IL-4 and IL-13 are interesting targets for allergy and asthma therapies. Knowledge of the binding mechanism will be important for the generation of either IL-4 or IL-13 specific drugs.

PubMed: 16640778
DOI: 10.1186/1741-7007-4-13

Experimental method

X-RAY DIFFRACTION (2.1 Å)