Abstract:
:Insulin receptors (IRs) that are truncated at the end of the ectodomain form dimers that bind insulin with different characteristics to wild type receptors. These soluble IRs have lowered affinity for insulin compared with full-length IR, and exhibit linear Scatchard plots in contrast to the curvilinear plots obtained with full-length IR, IR truncated at the C-terminus of the transmembrane region and IR ectodomains fused to the self-associating constant domains from Fc or lambda immunoglobulins. In this report, we have fused the IR ectodomain to the 33 residue leucine zipper from the transcriptional activator GCN4 of Saccharomyces cerevisiae. This fusion protein binds insulin with high affinity in a manner comparable to native receptor. The respective dissociation constants were Kd1 8.2 X 10(-11) M and Kd2 1.6 x 10(-8) M for hIRedZip and Kd1 5.7 x 10(-11) M and Kd2 6.3 x 10(-9) M for membrane-anchored, native receptor.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Hoyne PA,Cosgrove LJ,McKern NM,Bentley JD,Ivancic N,Elleman TC,Ward CWdoi
10.1016/s0014-5793(00)01872-xkeywords:
subject
Has Abstractpub_date
2000-08-11 00:00:00pages
15-8issue
1-2eissn
0014-5793issn
1873-3468pii
S0014-5793(00)01872-Xjournal_volume
479pub_type
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