Rescue of ligand binding of a mutant IGF-I receptor by complementation.

Abstract:

:The IGF-I receptor binds IGF-I with complex kinetics characterized by a curvilinear Scatchard plot, suggesting receptor heterogeneity and apparent negative cooperativity. To explore the molecular mechanisms underlying these properties, we have characterized the binding of a hybrid receptor formed from a wild-type receptor monomer and a mutant receptor monomer devoid of binding activity. Receptor hybrids were generated by transient co-transfection of cDNAs encoding wild-type and mutant receptors with unique epitope tags. Hybrid receptors were purified from transfected cells by sequential immuno-affinity chromatography and their ligand-binding properties were determined. Complementation produced a hybrid with near wild-type affinity. Dissociation studies demonstrated that the hybrid did not exhibit negative cooperativity.

authors

Chakravarty A,Hinrichsen J,Whittaker L,Whittaker J

doi

10.1016/j.bbrc.2005.03.122

subject

Has Abstract

pub_date

2005-05-27 00:00:00

pages

74-7

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(05)00641-8

journal_volume

331

pub_type

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