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Always look on the bright site of Rho: structural implications for a conserved intermolecular interface
Author(s) -
Dvorsky Radovan,
Ahmadian Mohammad Reza
Publication year - 2004
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1038/sj.embor.7400293
Subject(s) - gtpase , biology , function (biology) , conserved sequence , effector , computational biology , intermolecular force , microbiology and biotechnology , peptide sequence , genetics , chemistry , gene , molecule , organic chemistry
The signalling functions of Rho‐family GTPases are based on the formation of distinctive protein–protein complexes. Invaluable insights into the structure–function relationships of the Rho GTPases have been obtained through the resolution of several of their structures in complex with regulators and downstream effectors. In this review, we use these complexes to compare the binding and specificity‐determining sites of the Rho GTPases. Although the properties that characterize these sites are diverse, some fundamental conserved principles that govern their intermolecular interactions have emerged. Notably, all of the interacting partners of the Rho GTPases, irrespective of their function, bind to a common set of conserved amino acids that are clustered on the surface of the switch regions. This conserved region and its specific structural characteristics exemplify the convergence of the Rho GTPases on a consensus binding site.