Disease relevance of IL2RG

• 2. When p64 and three p64 Staphylococcus aureus V8 proteolytic fragments were sequenced, the same N-termini sequence was obtained: Ala-Pro-Ile-Thr-Asp-Ala-Asp-Leu-Gly-Pro-Ala-Gln-Ile-Ala-Asp, which displayed a significant homology with a putative Trypanosoma brucei VSG gene located on chromosome 4 [1].
• We have raised a polyclonal antibody to an E. coli fusion protein which has sequence similarity to p64 [2].

High impact information on IL2RG

• Molecular mass and sequence comparison confirm that Cep3p is the p64 component of centromere DNA binding complex Cbf3 (Lechner, 1994) [3].
• All preparations of p61 also contain a 64-kDa protein (p64) that is phosphorylated on tyrosine [4].
• Measurement of the Stokes radius of p61 and p64 by gel filtration shows that they are not physically associated in buffer containing the nonionic detergent Lubrol 12A9 [4].
• CLIC-1 is a member of a family of proteins related to the bovine intracellular chloride channel p64 which has been proposed to function as a chloride channel [5].
• The predicted amino acid sequence of p64 shows that it contains two and possibly four putative transmembrane domains and potential phosphorylation sites by protein kinase A, protein kinase C, and casein kinase II [6].

Biological context of IL2RG

• All these results together with prior evidences [Uzcanga, G. et al. (2002) Parasitology 124, 287-299] confirmed that p64 is the soluble form of a T. evansi VSG, containing common epitopes recognized by sera from animals infected with T. evansi or T. vivax [1].

Anatomical context of IL2RG

• It is likely that p64 represents the chloride channel of intracellular organelles [6].
• Molecular cloning and characterization of p64, a chloride channel protein from kidney microsomes [6].
• A 64-kDa protein, p64, identified as a component of this chloride channel was used to generate antibodies which depleted solubilized kidney membranes of all chloride channel activity [6].
• The crystal structure of gamma-crystallin IIIb (gamma C) from calf eye lens has been refined at 2.5 A resolution [7].

Associations of IL2RG with chemical compounds

• Isoelectric focusing and two-dimensional polyacrylamide gel electrophoresis revealed that p64 contained two isoforms with isoelectric points of 6.8-6.9 and 7.1-7 [1].

Analytical, diagnostic and therapeutic context of IL2RG

• Additionally, immunofluorescence microscopy on T. evansi and T. vivax established that p64 and its T. vivax homologue were confined to the surface of both parasites [1].

References