Work

Lack of association of G-protein β2- and γ2-subunit N-terminal fragments provides evidence against the coiled-coil model of subunit-βγ assembly

Year: 1995

Type: article

Abstract: The association between peptides from bovine G-protein beta 2- and gamma 2-subunits was studied by CD spectroscopy and cross-linking. Both peptides had approximately 25% stable alpha-helical structure at 25 degrees C, but there was no increase on mixing subunits as expected for coiled-coil formation. Also, disulphide cross-linking gave more beta 2 beta 2 homodimer than beta 2 gamma 2 heterodimer. These data do not support the proposed N-terminal coiled-coil model of beta gamma-subunit association.

Source: Biochemical Journal

DOI: 10.1042/bj3090377

Authors: E P Marin, R R Neubig

Institutions: University of Michigan, Michigan Medicine

Language: English

Topic: Receptor Mechanisms and Signaling

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: bronze

Funders: National Heart, Lung, and Blood Institute, National Institute of General Medical Sciences

Awards: G132595636, G2051615983, G2449357288, Michigan Medical Scientist Training Program, Physiological functions of G-alpha-i/o and control by regulators of G protein sig