title: The crystal structure of the tumor suppressor protein pp32 (Anp32a): structural insights into Anp32 family of proteins.
abstract: The tumor suppressor protein pp32 is highly overexpressed in many cancers of the breast and prostate, and has also been implicated in the neurodegenerative disease spinocerebellar ataxias type 1 (SCA1). Pp32 is a multifunctional protein that is involved in the regulation of transcription, apoptosis, phosphorylation, and cell cycle progression, the latter through its association with the hyperphosphorylated form of the retinoblastoma tumor suppressor. We have determined the structure of an N-terminal pp32 fragment comprising a capped leucine-rich repeat (LRR) domain, which provides insight into the structural and biochemical properties of the pp32 (Anp32) family of proteins.
authors.affiliation: Department of Biophysics and Biophysical Chemistry, Howard Hughes Medical Institute, Johns Hopkins University School of Medicine, Baltimore, MD 21205-2185, USA.
authors.forename: Trevor
authors.initials: T
authors.lastname: Huyton
authors.forename: Cynthia
authors.initials: C
authors.lastname: Wolberger
mesh_terms: D000595:Amino Acid Sequence; D018360:Crystallography, X-Ray; D006801:Humans; D047908:Intracellular Signaling Peptides and Proteins / Q000737:chemistry* / Q000235:genetics; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009687:Nuclear Proteins; D010446:Peptide Fragments / Q000737:chemistry* / Q000235:genetics; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D016601:RNA-Binding Proteins; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification; D017386:Sequence Homology, Amino Acid
chemical_list: C087425:ANP32A protein, human; D047908:Intracellular Signaling Peptides and Proteins; D009687:Nuclear Proteins; D010446:Peptide Fragments; D016601:RNA-Binding Proteins; D011994:Recombinant Proteins