A Point Mutation to Gαi Selectively Blocks GoLoco Motif Binding
نویسندگان
چکیده
منابع مشابه
Point mutation of adenosine triphosphate-binding motif generated rigor kinesin that selectively blocks anterograde lysosome membrane transport
In the study of motor proteins, the molecular mechanism of mechanochemical coupling, as well as the cellular role of these proteins, is an important issue. To assess these questions we introduced cDNA of wild-type and site-directed mutant kinesin heavy chains into fibroblasts, and analyzed the behavior of the recombinant proteins and the mechanisms involved in organelle transports. Overexpressi...
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Molecular dynamics simulations, computational alanine scanning and sequence analysis were used to investigate the structural properties of the Galpha(i1)/GoLoco peptide complex. Using these methodologies, binding of the GoLoco motif peptide to the Galpha(i1) subunit was found to restrict the relative movement of the helical and catalytic domains in the Galpha(i1) subunit, which is in agreement ...
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GoLoco ('Galpha(i/o)-Loco' interaction) motif proteins have recently been identified as novel GDIs (guanine nucleotide dissociation inhibitors) for heterotrimeric G-protein alpha subunits. G18 is a member of the mammalian GoLoco-motif gene family and was uncovered by analyses of human and mouse genomes for anonymous open-reading frames. The encoded G18 polypeptide is predicted to contain three ...
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Heterotrimeric G-protein alpha subunits (Gα) are molecular switches regulated by the binding and hydrolysis of guanosine 5-triphosphate [1]. Non-receptor proteins that modulate the nucleotide binding and hydrolysis activities of Gα proteins have recently become of considerable interest [2, 3]. One class of Gα modulating proteins is defined by the presence of a GoLoco motif(s) in their primary s...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2008
ISSN: 0021-9258
DOI: 10.1074/jbc.m804936200