3VOQ

Crystal structure of the pleckstrin homology domain of human Sin1, a TORC2 subunit

Summary for 3VOQ

Entry DOI	10.2210/pdb3voq/pdb
Related	3ULB 3ULC
Descriptor	Target of rapamycin complex 2 subunit MAPKAP1 (2 entities in total)
Functional Keywords	ph domain, membrane protein
Biological source	Homo sapiens (human)
Cellular location	Cell membrane; Peripheral membrane protein: Q9BPZ7
Total number of polymer chains	2
Total formula weight	28228.14
Authors	Pan, D.,Matsuura, Y. (deposition date: 2012-01-31, release date: 2012-04-11, Last modification date: 2023-11-08)
Primary citation	Pan, D.,Matsuura, Y. Structures of the pleckstrin homology domain of Saccharomyces cerevisiae Avo1 and its human orthologue Sin1, an essential subunit of TOR complex 2 Acta Crystallogr.,Sect.F, 68:386-392, 2012 Cited by PubMed 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. PubMed: 22505404 DOI: 10.1107/S1744309112007178 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2 Å)

Structure validation