Structure-Function Relationships of the G Domain, a Canonical Switch Motif

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 conform...

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Veröffentlicht in:	Annual review of biochemistry 2011-07, Vol.80 (1), p.943-971
Hauptverfasser:	Wittinghofer, Alfred, Vetter, Ingrid R
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Motifs Binding Sites Crystallography, X-Ray GTP binding domain GTP-Binding Proteins - chemistry GTP-Binding Proteins - genetics GTP-Binding Proteins - metabolism Guanosine Diphosphate - chemistry Guanosine Diphosphate - metabolism Guanosine Triphosphate - chemistry Guanosine Triphosphate - metabolism Humans Models, Molecular Molecular Sequence Data Molecular Structure molecular switch Molecules Protein Multimerization Protein Structure, Secondary Protein Structure, Tertiary Proteins Structure-Activity Relationship Substrate Specificity three-dimensional structure Topology
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Beschreibung
Zusammenfassung:	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.
ISSN:	0066-4154 1545-4509
DOI:	10.1146/annurev-biochem-062708-134043