1B3U

CRYSTAL STRUCTURE OF CONSTANT REGULATORY DOMAIN OF HUMAN PP2A, PR65ALPHA

Summary for 1B3U

• Entry DOI: 10.2210/pdb1b3u/pdb
• Descriptor: PROTEIN (PROTEIN PHOSPHATASE PP2A) (2 entities in total)
• Functional Keywords: scaffold protein, pp2a, phosphorylation, heat repeat
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 2
• Total formula weight: 130494.30

Authors

Groves, M.R.,Hanlon, N.,Turowski, P.,Hemmings, B.,Barford, D. (deposition date: 1998-12-14, release date: 1999-04-12, Last modification date: 2023-12-27)

Primary citation

Groves, M.R.,Hanlon, N.,Turowski, P.,Hemmings, B.A.,Barford, D.
The structure of the protein phosphatase 2A PR65/A subunit reveals the conformation of its 15 tandemly repeated HEAT motifs.
Cell(Cambridge,Mass.), 96:99-110, 1999

PubMed Abstract: The PR65/A subunit of protein phosphatase 2A serves as a scaffolding molecule to coordinate the assembly of the catalytic subunit and a variable regulatory B subunit, generating functionally diverse heterotrimers. Mutations of the beta isoform of PR65 are associated with lung and colon tumors. The crystal structure of the PR65/Aalpha subunit, at 2.3 A resolution, reveals the conformation of its 15 tandemly repeated HEAT sequences, degenerate motifs of approximately 39 amino acids present in a variety of proteins, including huntingtin and importin beta. Individual motifs are composed of a pair of antiparallel alpha helices that assemble in a mainly linear, repetitive fashion to form an elongated molecule characterized by a double layer of alpha helices. Left-handed rotations at three interrepeat interfaces generate a novel left-hand superhelical conformation. The protein interaction interface is formed from the intrarepeat turns that are aligned to form a continuous ridge.

PubMed: 9989501
DOI: 10.1016/S0092-8674(00)80963-0

Experimental method

X-RAY DIFFRACTION (2.3 Å)