1HZI

INTERLEUKIN-4 MUTANT E9A

Summary for 1HZI

• Entry DOI: 10.2210/pdb1hzi/pdb
• Related: 1hij 1hik 1iar 1rcb 2int
• Descriptor: INTERLEUKIN-4, SULFATE ION (3 entities in total)
• Functional Keywords: il-4, 4-helix-bundle, cytokine
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 15411.53

Authors

Hulsmeyer, M.,Scheufler, C.,Dreyer, M.K. (deposition date: 2001-01-25, release date: 2001-08-29, Last modification date: 2024-10-30)

Primary citation

Hulsmeyer, M.,Scheufler, C.,Dreyer, M.K.
Structure of interleukin 4 mutant E9A suggests polar steering in receptor-complex formation.
Acta Crystallogr.,Sect.D, 57:1334-1336, 2001

PubMed Abstract: Interleukin 4 (IL-4) is a pleiotropic cytokine which induces T-cell differentiation and class switching of B cells. It therefore plays a central role in the development of allergies and asthma. An IL-4 variant in which Glu9 was mutated to alanine shows an 800-fold drop in binding affinity towards its high-affinity receptor chain. As shown by surface plasmon resonance measurements, this mostly arises from a decreased association rate. Here, the crystal structure of this mutant is reported. It reveals that the protein has a virtually identical structure to the wild type, showing that the unusual behaviour of the mutated protein is not a consequence of misfolding. The possibility that polar interactions in the encounter complex have a steering effect is discussed.

PubMed: 11526337
DOI: 10.1107/S0907444901009799

Experimental method

X-RAY DIFFRACTION (2.05 Å)