Structures of the pleckstrin homology domain of Saccharomyces cerevisiae Avo1 and its human orthologue Sin1, an essential subunit of TOR complex 2.
In eukaryotes, multiprotein complexes termed TOR complex 1 (TORC1) and TOR complex 2 (TORC2) function as major regulators of cell growth, metabolism and ageing. The C-terminal domain of the Saccharomyces cerevisiae TORC2 component Avo1 is required for plasma-membrane localization of TORC2 and is essential for yeast viability. X-ray crystal structures of the C-terminal domain of Avo1 and of its human orthologue Sin1 have been determined. The structures show that the C-termini of Avo1 and Sin1 both have the pleckstrin homology (PH) domain fold. Comparison with known PH-domain structures suggests a putative binding site for phosphoinositides.
Division of Biological Science, Graduate School of Science, Nagoya University, Nagoya 464-8602, Japan.
SourceActa crystallographica. Section F, Structural biology and crystallization communications 68:Pt 4 2012 Apr 1 pg 386-92
MeSHAdaptor Proteins, Signal Transducing
Amino Acid Sequence
Molecular Sequence Data
Protein Structure, Quaternary
Protein Structure, Tertiary
Saccharomyces cerevisiae Proteins
Structural Homology, Protein
Pub Type(s)Journal Article