PDBsum entry: 2je1

Nuclear protein

PDB id: 2je1

Contents

Protein chains

149 a.a. *

Ligands

GOL

Waters ×145

* Residue conservation analysis

PDB id:

2je1

Name:

Nuclear protein

Title:

The crystal structure of the tumor supressor protein pp32 ( anp32a):structural insights into the anp32 family of proteins

Structure:

Acidic leucine-rich nuclear phosphoprotein 32 fam member a. Chain: a, b, c, d. Fragment: lrr domain, residues 1-149. Synonym: potent heat-stable protein phosphatase 2a inhibito i1pp2a, acidic nuclear phosphoprotein pp32, leucine-rich a nuclear protein, lanp, putative hla-dr-associated protein phapi, mapmodulin, pp32. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

2.69Å R-factor: 0.241 R-free: 0.303

Authors:

T.Huyton,C.Wolberger

Key ref:

T.Huyton and C.Wolberger (2007). The crystal structure of the tumor suppressor protein pp32 (Anp32a): structural insights into Anp32 family of proteins. Protein Sci, 16, 1308-1315. PubMed id: 17567741 DOI: 10.1110/ps.072803507

Date:

12-Jan-07 Release date: 26-Jun-07

Protein chains

P39687  (AN32A_HUMAN) -  Acidic leucine-rich nuclear phosphoprotein 32 family member A

Seq: 249 a.a.

Struc: 149 a.a.

 Gene Ontology (GO) functional annotation 

• Biochemical function: protein binding (1 term)

DOI no: 10.1110/ps.072803507

Protein Sci 16:1308-1315 (2007)

PubMed id: 17567741

The crystal structure of the tumor suppressor protein pp32 (Anp32a): structural insights into Anp32 family of proteins.

T.Huyton, C.Wolberger.

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.

Selected figure(s)

Figure 1.
Figure 1. (A) Stereo ribbon representation of the structure of pp32DCT illustrating the canonical curved structure of the LRR domain.

The above figure is reprinted by permission from the Protein Society: Protein Sci (2007, 16, 1308-1315) copyright 2007.

Figure was selected by an automated process.