Title : Structural analysis of recombinant soluble human
interleukin-2 receptor
Abstract :
- Primary structure, assignment of disulfide bonds and core IL-2 binding structure
- A purified soluble and functional form of recombinant human interleukin-2 receptor , engineered and expressed in Chinese hamster ovary cells, was structurally characterized
- The primary sequence of this 224 amino acid recombinant protein which lacks most of the carboxy-terminal transmembrane and cytoplasmic portions of the intact protein was established by sequence analyses
- The disulfide bonds were assigned by comparative peptide mapping of the reduced and non-reduced peptide digests
- As in the case of natural interleukin-2 receptor they occur between cysteines 3-147, 46-104, 131-163 , and 28/30-59/61
- Based on assignment of the disulfide bonds, a structural model of the interleukin-2 receptor for interleukin-2 binding is proposed
Output (sent_index, trigger,
protein,
sugar,
site):
Output(Part-Of) (sent_index,
protein,
site):
*Output_Site_Fusion* (sent_index,
protein,
sugar,
site):