Crystal structure of the interleukin-4/receptor alpha chain complex reveals a mosaic binding interface

Article Abstract:

The interaction between interleukin-4 (IL-4) and its receptor alpha chain (IL-4BP) is needed to generate a Th2-dominated early immune response. An examination of the IL4/IL-4BP interaction indicates that an intermediate complex is formed, one that recruits the common gamma chain to initiate transmembrane signaling. The crystal structure of this intermediate complex is described at 2.3 Angstrom resolution. The structure has a novel spatial arrangement, an unexpected conformational change at the receptor-bound IL-4 and a mosaic binding interface with three clusters of residues.

Proteins, Cell receptors, Protein structure, Interleukin-4

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Solution structure and ligand-binding site of the SH3 domain of the p85-alpha subunit of phosphatidylinositol 3-kinase

Article Abstract:

A study to characterize the solution structure and ligand-binding site of the SH3 domain of the 85-kD regulatory subunit (p85-alpha) of phosphatidylinositol 3-kinase is reported. Proteins associated with receptor tyrosine kinase signal transduction pathways possess SH3 domains which could have intrinsic enzymatic or regulatory activities. The solution structure of p85-alpha shows that it belongs to a separate class of SH3 domain structure. Its ligand-binding site consists of two charged loops flanking a hydrophobic surface.

Analysis, Protein tyrosine kinase, Protein-tyrosine kinase

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Gene targeting: attention to detail

Article Abstract:

A prime example highlighting ho\w different gene inactivation strategies can lead to striking different phenotypes is presented. The conclusion suggests that caution should be used when validating potential drug targets by genetic disruption.

Product information, Science & research, Testing, Phenotype, Phenotypes, Gene amplification, Gene targeting

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