3VOQ: Crystal Structure Of The Pleckstrin Homology Domain Of Human Sin1, A Torc2 Subunit

Citation:
Abstract
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.
PDB ID: 3VOQDownload
MMDB ID: 98718
PDB Deposition Date: 2012/1/31
Updated in MMDB: 2013/08
Experimental Method:
x-ray diffraction
Resolution: 2  Å
Source Organism:
Similar Structures:
Biological Unit for 3VOQ: dimeric; determined by author and by software (PISA)
Molecular Components in 3VOQ
Label Count Molecule
Proteins (2 molecules)
2
Target of Rapamycin Complex 2 Subunit Mapkap1(Gene symbol: MAPKAP1)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB
.