Structure-Function Relationships of the G Domain, a Canonical Switch Motif
2011; Annual Reviews; Volume: 80; Issue: 1 Linguagem: Inglês
10.1146/annurev-biochem-062708-134043
ISSN1545-4509
AutoresAlfred Wittinghofer, Ingrid R. Vetter,
Tópico(s)Enzyme Structure and Function
ResumoGTP-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.
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