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Annu Rev Biochem. 2011;80:943-71. doi: 10.1146/annurev-biochem-062708-134043.

Structure-function relationships of the G domain, a canonical switch motif.

Author information

1
Max Planck Institut für Molekulare Physiologie, 44227 Dortmund, Germany. ingrid.vetter@mpi-dortmund.mpg.de

Abstract

GTP-binding (G) proteins constitute a class of P-loop (phosphate-binding loop) proteins that work as molecular switches between the GDP-bound OFF and the GTP-bound ON state. The common principle is the 160-180-residue G domain with an α,β topology that is responsible for nucleotide-dependent conformational changes and drives many biological functions. Although the G domain uses a universally conserved switching mechanism, its structure, function, and GTPase reaction are modified for many different pathways and processes.

[Indexed for MEDLINE]

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